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Protein

Putative succinate-semialdehyde dehydrogenase C1002.12c [NADP(+)]

Gene

SPAC1002.12c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H.

Pathwayi: 4-aminobutanoate degradation

This protein is involved in the pathway 4-aminobutanoate degradation, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway 4-aminobutanoate degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei318 – 3181PROSITE-ProRule annotation
Active sitei352 – 3521PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi296 – 3016NAD or NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-SPO-916853. Degradation of GABA.
UniPathwayiUPA00733.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative succinate-semialdehyde dehydrogenase C1002.12c [NADP(+)] (EC:1.2.1.16)
Short name:
SSDH
Gene namesi
ORF Names:SPAC1002.12c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1002.12c.
PomBaseiSPAC1002.12c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Putative succinate-semialdehyde dehydrogenase C1002.12c [NADP(+)]PRO_0000310351Add
BLAST

Proteomic databases

MaxQBiQ9US47.
PRIDEiQ9US47.

Interactioni

Protein-protein interaction databases

BioGridi279695. 10 interactions.
MINTiMINT-4707707.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

HOGENOMiHOG000271509.
InParanoidiQ9US47.
KOiK00135.
OMAiPVAKMLY.
OrthoDBiEOG7S226Z.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010102. Succ_semiAld_DH.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01780. SSADH. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9US47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSLIQSIPR YIYESNSLPK LIRSGLDRKS PIGLSLLKRN CRNRSFAANM
60 70 80 90 100
STSSKLSTNI KDLSLFDLEE FPARSYIGGK WVTAASGKTF DVENPGLNET
110 120 130 140 150
LAPVTDMSVE ETRKAIKVAH EAFLSYRNSD IKERYAILRR WYDLIMENAD
160 170 180 190 200
DLATMMTLEN GKALGDAKGE VVYAAKFIDW FAGEALRISG DSSMSSNPQN
210 220 230 240 250
RIITIKQPVG VVGIITPWNF PAAMITRKVG AALAAGCTVV IRPAAETPFT
260 270 280 290 300
ALALAKLAER AGVPAGVLNM VTANSPSEHG IELTTNPLIR KVSFTGSTNV
310 320 330 340 350
GKILAKQSSS TLKKLSLELG GNAPFIVFED ADLEKAADAL MACKFRGSGQ
360 370 380 390 400
TCVCANRIYV HSSVYDAFVD LVTERVSKFK LGYGLDAGVT HGPLISEKAI
410 420 430 440 450
SKVKQHVEDA VQKGGVVVTG GKVASNLGPM YFEPTVIINA KQGMLISEEE
460 470 480 490 500
TFGPVGALFK FDTEDEVVAW ANDSPVGLAG YLFSKDISRV FRVGEALQVG
510 520 530 540
MVGCNTGLVS DVLSPFGGVK ESGFGREGSK YGISEYLDIK SLTISTL
Length:547
Mass (Da):58,834
Last modified:June 13, 2012 - v2
Checksum:i8AD9B9A48C768252
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB65612.2.
RefSeqiNP_593499.2. NM_001018933.2.

Genome annotation databases

EnsemblFungiiSPAC1002.12c.1; SPAC1002.12c.1:pep; SPAC1002.12c.
GeneIDi2543267.
KEGGispo:SPAC1002.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB65612.2.
RefSeqiNP_593499.2. NM_001018933.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279695. 10 interactions.
MINTiMINT-4707707.

Proteomic databases

MaxQBiQ9US47.
PRIDEiQ9US47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1002.12c.1; SPAC1002.12c.1:pep; SPAC1002.12c.
GeneIDi2543267.
KEGGispo:SPAC1002.12c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1002.12c.
PomBaseiSPAC1002.12c.

Phylogenomic databases

HOGENOMiHOG000271509.
InParanoidiQ9US47.
KOiK00135.
OMAiPVAKMLY.
OrthoDBiEOG7S226Z.

Enzyme and pathway databases

UniPathwayiUPA00733.
ReactomeiR-SPO-916853. Degradation of GABA.

Miscellaneous databases

NextBioi20804288.
PROiQ9US47.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010102. Succ_semiAld_DH.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01780. SSADH. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSSDH1_SCHPO
AccessioniPrimary (citable) accession number: Q9US47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 13, 2012
Last modified: May 11, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.