(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIK4_GEOS0

ID   A0A0F6BIK4_GEOS0        Unreviewed;       335 AA.
AC   A0A0F6BIK4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 34.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   OrderedLocusNames=GY4MC1_0414 {ECO:0000313|EMBL:ADP73255.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73255.1};
RN   [1] {ECO:0000313|EMBL:ADP73255.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73255.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; CP002293; ADP73255.1; -; Genomic_DNA.
DR   RefSeq; WP_003248107.1; NC_014650.1.
DR   EnsemblBacteria; ADP73255; ADP73255; GY4MC1_0414.
DR   GeneID; 29236926; -.
DR   KEGG; gmc:GY4MC1_0414; -.
DR   KO; K00134; -.
DR   OMA; DSTHGHF; -.
DR   OrthoDB; 944149at2; -.
DR   BioCyc; GSP581103:G1GOQ-461-MONOMER; -.
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; IPR036291; NAD(P)-bd_dom_sf.
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; A0A0F6BIK4.
DR   SWISS-2DPAGE; A0A0F6BIK4.
KW   NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361160,
KW   ECO:0000313|EMBL:ADP73255.1}.
FT   DOMAIN          3..152
FT                   /note="Gp_dh_N"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NP_BIND         12..13
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   REGION          151..153
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   REGION          210..211
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         34
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         78
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         120
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         182
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         233
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         315
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            179
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ   SEQUENCE   335 AA;  36134 MW;  EFE482574E0F055C CRC64;
     MAVKIGINGF GRIGRNVFRA ALKNPNIEVV AVNDLTDANT LAHLLKYDSV HGKLDAEVSV
     NGNNIVVNGK EIVVKAERDP AQLAWNELGV DIVVESTGRF TKREDAAKHL EAGAKKVIIS
     APAKNEDITI VMGVNQDKYD PANHHIISNA SCTTNCLAPF AKVLHEKFGI VRGMMTTVHS
     YTNDQQILDL PHKDLRRARA AAESIIPTTT GAAKAVALVL PELKGKLNGM AMRVPTPNVS
     VVDLVAELEK EVTVEEVNAA LKEAAEGELK GILAYSEEPL VSRDYNGSTV SSTIDALSTM
     VIEGTMVKVV SWYDNETGYS HRVVDLAEYI ASKGL
//

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