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Database: UniProt
Entry: A0A0S2JIP4_9GAMM
LinkDB: A0A0S2JIP4_9GAMM
Original site: A0A0S2JIP4_9GAMM 
ID   A0A0S2JIP4_9GAMM        Unreviewed;       350 AA.
AC   A0A0S2JIP4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   ORFNames=CMT41_14315 {ECO:0000313|EMBL:ALO35760.1};
OS   Colwellia sp. MT41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO35760.1, ECO:0000313|Proteomes:UP000065319};
RN   [1] {ECO:0000313|EMBL:ALO35760.1, ECO:0000313|Proteomes:UP000065319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MT41 {ECO:0000313|EMBL:ALO35760.1,
RC   ECO:0000313|Proteomes:UP000065319};
RA   Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA   Yayanos A., Methe B.A., Bartlett D.H.;
RT   "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT   Colwellia.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; CP013145; ALO35760.1; -; Genomic_DNA.
DR   RefSeq; WP_058027653.1; NZ_CP013145.1.
DR   AlphaFoldDB; A0A0S2JIP4; -.
DR   STRING; 58049.CMT41_14315; -.
DR   KEGG; com:CMT41_14315; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000065319; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; NF033735; G3PDH_Arsen; 1.
DR   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR42955; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42955:SF1; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065319}.
FT   DOMAIN          3..162
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        162
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         161..163
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         192
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         220..221
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         243
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         325
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            189
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ   SEQUENCE   350 AA;  38418 MW;  8E77C85827624548 CRC64;
     MTIKVGINGF GRMGRLILRA AWHWPEIEFI QINDPAGDAP TLAHLLNFDS IHGRWQYEAT
     ATAKLMYIEG KTLHVSQNEG LAETDWSGCD IVIEASGVMR DKAKLQAYFL QGVKKVLVTA
     PMKIAQDSSG NILDKDIVNI VMGVNQQLYQ GEQHSIVTAA SCTTNCLAPV IKVLQDNIGI
     KHGSMTTIHN VTNTQTILDA PHKDLRRARA CGQSLIPTTT GSAKAITDIF PELKGKLNGH
     AVRVPLANAS LTDCVFEMQR DVTVEEVNQL MADAAAGELN GILGYEERPL VSVDYKTDTR
     SCVVDALSTM VINGTQLKMY LWYDNEWGYA NRSAELMKII ALSLTDINES
//
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