(data stored in ACNUC7421 zone)

SWISSPROT: A8FQR5_SHESH

ID   A8FQR5_SHESH            Unreviewed;       353 AA.
AC   A8FQR5;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 69.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   OrderedLocusNames=Ssed_0576 {ECO:0000313|EMBL:ABV35188.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35188.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35188.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35188.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; CP000821; ABV35188.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8FQR5; -.
DR   STRING; 425104.Ssed_0576; -.
DR   EnsemblBacteria; ABV35188; ABV35188; Ssed_0576.
DR   KEGG; sse:Ssed_0576; -.
DR   eggNOG; COG0057; LUCA.
DR   HOGENOM; HOG000071679; -.
DR   KO; K00134; -.
DR   OMA; VACPVKG; -.
DR   OrthoDB; POG091H02BL; -.
DR   BioCyc; SSED425104:GH7Q-598-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQR5.
DR   SWISS-2DPAGE; A8FQR5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361160,
KW   ECO:0000313|EMBL:ABV35188.1}.
FT   DOMAIN       20    169       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
FT   REGION      168    170       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   REGION      227    228       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   ACT_SITE    169    169       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR000149-1}.
FT   BINDING     199    199       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   BINDING     250    250       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   SITE        196    196       Activates thiol group during catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000149-4}.
SQ   SEQUENCE   353 AA;  38588 MW;  E4AA3597D278A4EF CRC64;
     MGLEDHITRE DRIKGFNMSI KIGINGFGRM GRLALRAAWD WDDVEFVQIN DPAGDAATLA
     HLLTFDSIHG RWHHEATGEG SEIRIGDTRI ATTQDSNIGD TDWSGCDLVI EASGVMKTKA
     LLQAYIDQGV KRVVVTAPVK EEGVLNVVMG VNHHLYDKSL HPIVTAASCT TNCLAPVVKV
     IHETIGIKHG SMTTIHDITN TQTILDAPHK DLRRARACGL SLIPTTTGSA TAITHIFPEL
     KGKLNGHAVR VPLANASITD CVFELEHATT EDEINALLKK AAEGELKDIM GYEERPLVSV
     DYKTDPRSCI IDAPSTMVVN GTQVKLYVWY DNEWGYANRT AELARMVGLS DKG
//

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