SSDH1_SCHPO
ID SSDH1_SCHPO Reviewed; 547 AA.
AC Q9US47;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative succinate-semialdehyde dehydrogenase C1002.12c [NADP(+)];
DE Short=SSDH;
DE EC=1.2.1.16;
GN ORFNames=SPAC1002.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.16;
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB65612.2; -; Genomic_DNA.
DR RefSeq; NP_593499.2; NM_001018933.2.
DR AlphaFoldDB; Q9US47; -.
DR SMR; Q9US47; -.
DR BioGRID; 279695; 11.
DR STRING; 4896.SPAC1002.12c.1; -.
DR MaxQB; Q9US47; -.
DR PaxDb; Q9US47; -.
DR EnsemblFungi; SPAC1002.12c.1; SPAC1002.12c.1:pep; SPAC1002.12c.
DR GeneID; 2543267; -.
DR KEGG; spo:SPAC1002.12c; -.
DR PomBase; SPAC1002.12c; -.
DR VEuPathDB; FungiDB:SPAC1002.12c; -.
DR eggNOG; KOG2451; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; Q9US47; -.
DR OMA; IKYICMS; -.
DR Reactome; R-SPO-916853; Degradation of GABA.
DR UniPathway; UPA00733; -.
DR PRO; PR:Q9US47; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR GO; GO:0006540; P:glutamate decarboxylation to succinate; ISO:PomBase.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010102; Succ_semiAld_DH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01780; SSADH; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..547
FT /note="Putative succinate-semialdehyde dehydrogenase
FT C1002.12c [NADP(+)]"
FT /id="PRO_0000310351"
FT ACT_SITE 318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 296..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 58834 MW; 8AD9B9A48C768252 CRC64;
MTSLIQSIPR YIYESNSLPK LIRSGLDRKS PIGLSLLKRN CRNRSFAANM STSSKLSTNI
KDLSLFDLEE FPARSYIGGK WVTAASGKTF DVENPGLNET LAPVTDMSVE ETRKAIKVAH
EAFLSYRNSD IKERYAILRR WYDLIMENAD DLATMMTLEN GKALGDAKGE VVYAAKFIDW
FAGEALRISG DSSMSSNPQN RIITIKQPVG VVGIITPWNF PAAMITRKVG AALAAGCTVV
IRPAAETPFT ALALAKLAER AGVPAGVLNM VTANSPSEHG IELTTNPLIR KVSFTGSTNV
GKILAKQSSS TLKKLSLELG GNAPFIVFED ADLEKAADAL MACKFRGSGQ TCVCANRIYV
HSSVYDAFVD LVTERVSKFK LGYGLDAGVT HGPLISEKAI SKVKQHVEDA VQKGGVVVTG
GKVASNLGPM YFEPTVIINA KQGMLISEEE TFGPVGALFK FDTEDEVVAW ANDSPVGLAG
YLFSKDISRV FRVGEALQVG MVGCNTGLVS DVLSPFGGVK ESGFGREGSK YGISEYLDIK
SLTISTL
