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protein coding gene - lys1 (SPAP7G5.04c) - aminoadipate-semialdehyde dehydrogenase

Gene summary

Standard name
lys1
Systematic ID
SPAP7G5.04c
Product
aminoadipate-semialdehyde dehydrogenase
Organism
Schizosaccharomyces pombe (fission yeast)
UniProt ID
P40976
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome I: 3739076..3743449 reverse strand

Annotation

Complementation

PBO:0017736 - functionally complemented by S. cerevisiae LYS2

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GO biological process

GO:0009085 - L-lysine biosynthetic process

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GO cellular component

GO:0005829 - cytosol

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GO molecular function

GO:0004043 - L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity

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GO:0031177 - phosphopantetheine binding

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Modification

MOD:00046 - O-phospho-L-serine

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MOD:00047 - O-phospho-L-threonine

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MOD:00159 - O-phosphopantetheine-L-serine

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MOD:00696 - phosphorylated residue

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MOD:01148 - ubiquitinylated lysine

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Multi-locus phenotype

FYPO:0002061 - inviable vegetative cell population

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Genotypes:

Protein sequence feature

SO:0001812 - transmembrane_helix

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Qualitative gene expression

PomGeneEx:0000019 - protein level decreased

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PomGeneEx:0000012 - RNA level decreased

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PomGeneEx:0000011 - RNA level increased

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Quantitative gene expression

PBO:0006310 - protein level

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PBO:0011963 - RNA level

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Single locus phenotype

FYPO:0004908 - abolished L-aminoadipate-semialdehyde dehydrogenase activity

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Genotypes:

FYPO:0000080 - decreased cell population growth at low temperature

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Genotypes:

FYPO:0009078 - decreased cell population growth on ethanol carbon source

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Genotypes:

FYPO:0002924 - decreased cell population growth on maltose carbon source

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Genotypes:

FYPO:0001176 - decreased cell population growth on sucrose carbon source

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Genotypes:

FYPO:0002725 - decreased L-aminoadipate-semialdehyde dehydrogenase activity

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Genotypes:

FYPO:0000039 - growth auxotrophic for lysine

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Genotypes:

FYPO:0005258 - increased cell population growth at high temperature

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Genotypes:

FYPO:0005261 - increased cell population growth on galactose carbon source

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Genotypes:

FYPO:0009093 - increased cell population growth on lysine and serine nitrogen source

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Genotypes:

FYPO:0009028 - increased cell population growth on proline nitrogen source

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Genotypes:

FYPO:0009074 - increased cell population growth on serine nitrogen source

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Genotypes:

FYPO:0001675 - increased L-aminoadipate-semialdehyde dehydrogenase activity

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Genotypes:

FYPO:0001309 - increased viability in stationary phase

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Genotypes:

FYPO:0000245 - loss of viability in stationary phase

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Genotypes:

FYPO:0009031 - resistance to bleomycin

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Genotypes:

FYPO:0000764 - resistance to cycloheximide

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Genotypes:

FYPO:0001103 - resistance to hydrogen peroxide

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Genotypes:

FYPO:0009085 - resistance to lithium chloride and sodium dodecyl sulfate

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Genotypes:

FYPO:0000077 - resistance to rapamycin

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Genotypes:

FYPO:0005968 - resistance to sodium chloride

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Genotypes:

FYPO:0000327 - resistance to trichostatin A

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Genotypes:

FYPO:0007933 - sensitive to 2,2′-dipyridyl

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Genotypes:

FYPO:0001501 - sensitive to brefeldin A

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Genotypes:

FYPO:0000097 - sensitive to caffeine during vegetative growth

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Genotypes:

FYPO:0000104 - sensitive to cycloheximide

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Genotypes:

FYPO:0000799 - sensitive to diamide

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Genotypes:

FYPO:0007931 - sensitive to egtazic acid

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Genotypes:

FYPO:0000842 - sensitive to ethanol during vegetative growth

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Genotypes:

FYPO:0007928 - sensitive to ethylenediaminetetraacetic acid

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Genotypes:

FYPO:0000785 - sensitive to formamide

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Genotypes:

FYPO:0000088 - sensitive to hydroxyurea

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Genotypes:

FYPO:0009071 - sensitive to itraconazole

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Genotypes:

FYPO:0001719 - sensitive to lithium

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Genotypes:

FYPO:0006836 - sensitive to magnesium chloride

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Genotypes:

FYPO:0009088 - sensitive to magnesium chloride and sodium dodecyl sulfate

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Genotypes:

FYPO:0000089 - sensitive to methyl methanesulfonate

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Genotypes:

FYPO:0001214 - sensitive to potassium chloride

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Genotypes:

FYPO:0007924 - sensitive to potassium chloride and sodium dodecyl sulfate

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Genotypes:

FYPO:0000797 - sensitive to tert-butyl hydroperoxide

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Genotypes:

FYPO:0002701 - sensitive to torin1

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Genotypes:

FYPO:0001457 - sensitive to tunicamycin

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Genotypes:

FYPO:0003656 - sensitive to vanadate

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Genotypes:

FYPO:0001234 - slow vegetative cell population growth

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Genotypes:

FYPO:0002060 - viable vegetative cell population

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Genotypes:

FYPO:0002177 - viable vegetative cell with normal cell morphology

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Genotypes:

Taxonomic conservation

PBO:0011067 - conserved in bacteria

PBO:0011065 - conserved in eukaryotes

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

PBO:0006222 - predominantly single copy (one to one)

Protein features

IDNameInterPro nameDB name
PF00501AMP-bindingAMP-dep_synth/lig_domPfam
PF00550PP-bindingPP-bd_ACPPfam
PF00668CondensationCondensation_domPfam
PF07993NAD_binding_4FAR_NAD-bdPfam
cd05235SDR_e1Thioester_reductase-like_domCDD
PS00012PHOSPHOPANTETHEINEPpantetheine_attach_sitePROSITE patterns
PS00455AMP_BINDINGAMP-binding_CSPROSITE patterns
PS50075CARRIERPP-bd_ACPPROSITE profiles
SM00823PKS_PPPKS_PP-bdSMART
G3DSA:3.30.559.30:FF:000068CATH-FunFam
G3DSA:3.40.50.720:FF:000787CATH-FunFam
G3DSA:1.10.1200.10ACP-like_sfCATH-Gene3D
G3DSA:3.30.300.30AMP-b_sfCATH-Gene3D
G3DSA:3.30.559.30CATH-Gene3D
G3DSA:3.40.50.12780ANL_N_sfCATH-Gene3D
G3DSA:3.40.50.720CATH-Gene3D
SSF47336ACP-like_sfSUPERFAMILY
SSF51735NAD(P)-bd_dom_sfSUPERFAMILY
SSF52777SUPERFAMILY
SSF56801SUPERFAMILY
PTHR44845PANTHER
PIRSF001617Alpha-ARPIRSF
TIGR01733AA-adenyl-domAA_adenyl_domNCBIFAM
TIGR01746Thioester-redctThioester_reductase-like_domNCBIFAM
TIGR03443alpha_am_amidLys2NCBIFAM

Orthologs

References / Literature

PMID:16823372 - ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Matsuyama A et al. Nat Biotechnol 2006 Jul;24(7):841-7
PMID:3142867 - Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe.
Ye ZH et al. J Bacteriol 1988 Dec;170(12):5968-70
PMID:24192486 - The conserved Fanconi anemia nuclease Fan1 and the SUMO E3 ligase Pli1 act in two novel Pso2-independent pathways of DNA interstrand crosslink repair in yeast.
Fontebasso Y et al. DNA Repair (Amst) 2013 Dec;12(12):1011-23
GO_REF:0000002 - Comments
PMID:25452419 - Parallel profiling of fission yeast deletion mutants for proliferation and for lifespan during long-term quiescence.
Sideri T et al. G3 (Bethesda) 2014 Dec 01;5(1):145-55
PMID:17248775 - Genetic Mapping in SCHIZOSACCHAROMYCES POMBE by Mitotic and Meiotic Analysis and Induced Haploidization.
Kohli J et al. Genetics 1977 Nov;87(3):471-89
PMID:27984744 - Survival in Quiescence Requires the Euchromatic Deployment of Clr4/SUV39H by Argonaute-Associated Small RNAs.
Joh RI et al. Mol Cell 2016 Dec 15;64(6):1088-1101
PMID:30726745 - Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.
Tay YD et al. Cell Rep 2019 Feb 05;26(6):1654-1667.e7
PMID:20537132 - Global fitness profiling of fission yeast deletion strains by barcode sequencing.
Han TX et al. Genome Biol 2010;11(6):R60
PMID:34250083 - Barcode sequencing and a high-throughput assay for chronological lifespan uncover ageing-associated genes in fission yeast.
Romila CA et al. Microb Cell 2021 Jul 05;8(7):146-160
PMID:37787768 - Broad functional profiling of fission yeast proteins using phenomics and machine learning.
Rodríguez-López M et al. Elife 2023 Oct 03;12
PMID:8350245 - Physical and functional characterization of the cloned lys1+ gene of Schizosaccharomyces pombe.
Ford RA et al. J Basic Microbiol 1993;33(3):179-86
PMID:35820914 - Antagonistic effects of mitochondrial matrix and intermembrane space proteases on yeast aging.
Vega M et al. BMC Biol 2022 Jul 12;20(1):160
PMID:39367033 - Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.
Sivakova B et al. Sci Rep 2024 Oct 04;14(1):23105
PMID:12136010 - Role of the Tsc1-Tsc2 complex in signaling and transport across the cell membrane in the fission yeast Schizosaccharomyces pombe.
Matsumoto S et al. Genetics 2002 Jul;161(3):1053-63
PMID:36478272 - Translation-complex profiling of fission yeast cells reveals dynamic rearrangements of scanning ribosomal subunits upon nutritional stress.
Duncan CDS et al. Nucleic Acids Res 2022 Dec 09;50(22):13011-13025
PMID:26412298 - A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.
Beckley JR et al. Mol Cell Proteomics 2015 Dec;14(12):3132-41
PMID:19547744 - Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species.
Beltrao P et al. PLoS Biol 2009 Jun 16;7(6):e1000134
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
PMID:29996109 - Quantitative Phosphoproteomics Reveals the Signaling Dynamics of Cell-Cycle Kinases in the Fission Yeast Schizosaccharomyces pombe.
Swaffer MP et al. Cell Rep 2018 Jul 10;24(2):503-514
PMID:36408920 - UniProt: the Universal Protein Knowledgebase in 2023.
UniProt Consortium Nucleic Acids Res 2023 Jan 06;51(D1):D523-D531
PMID:8590464 - Molecular properties of the lys1+ gene and the regulation of alpha-aminoadipate reductase in Schizosaccharomyces pombe.
Ford RA et al. Curr Genet 1995 Jul;28(2):131-7
PMID:8590485 - The Saccharomyces cerevisiae HIS3 and LYS2 genes complement the Schizosaccharomyces pombe his5-303 and lys1-131 mutations, respectively: new selectable markers and new multi-purpose multicopy shuttle vectors, pSP3 and pSP4.
Cottarel G Curr Genet 1995 Sep;28(4):380-3
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623
PMID:9559555 - Nucleotide sequence of the Schizosaccharomyces pombe lys1+ gene and similarities of the lys1+ protein to peptide antibiotic synthetases.
Bhattacherjee V et al. Yeast 1998 Mar 30;14(5):479-84
PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:39476757 - Characterization of Ksg1 protein kinase-dependent phosphoproteome in the fission yeast S. pombe.
Cipak L et al. Biochem Biophys Res Commun 2024 Oct 25;736:150895
PMID:15546125 - Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe.
Guo S et al. Yeast 2004 Nov;21(15):1279-88
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:16491385 - Cloning the Schizosaccharomyces pombe lys2+ gene and construction of new molecular genetic tools.
Hoffman RL et al. Curr Genet 2006 Jun;49(6):414-20
PMID:29432178 - General amino acid control in fission yeast is regulated by a nonconserved transcription factor, with functions analogous to Gcn4/Atf4.
Duncan CDS et al. Proc Natl Acad Sci U S A 2018 Feb 20;115(8):E1829-E1838
PMID:25720772 - Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.
Kettenbach AN et al. Mol Cell Proteomics 2015 May;14(5):1275-87
PMID:25375137 - Systematic analysis of the role of RNA-binding proteins in the regulation of RNA stability.
Hasan A et al. PLoS Genet 2014 Nov;10(11):e1004684
PMID:28218250 - Chromatin remodeller Fun30 Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation.
Lee J et al. Nat Commun 2017 Feb 20;8:14527
PMID:11152613 - Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes.
Krogh A et al. J Mol Biol 2001 Jan 19;305(3):567-80
PMID:39705284 - Proteomic and phosphoproteomic analyses reveal that TORC1 is reactivated by pheromone signaling during sexual reproduction in fission yeast.
Bérard M et al. PLoS Biol 2024 Dec 20;22(12):e3002963
PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83