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Database: UniProt
Entry: A0A1Y1R317_9GAMM
LinkDB: A0A1Y1R317_9GAMM
Original site: A0A1Y1R317_9GAMM 
ID   A0A1Y1R317_9GAMM        Unreviewed;       483 AA.
AC   A0A1Y1R317;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   ORFNames=B0D91_10190 {ECO:0000313|EMBL:OQX35780.1};
OS   Oceanospirillales bacterium LUC14_002_19_P2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX   NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX35780.1, ECO:0000313|Proteomes:UP000192421};
RN   [1] {ECO:0000313|EMBL:OQX35780.1, ECO:0000313|Proteomes:UP000192421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX35780.1};
RA   Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C., Campbell B.J.;
RT   "Novel co-symbiosis in the unique lucinid bivalve Phacoides pectinatus.";
RL   Submitted (FEB-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQX35780.1}.
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DR   EMBL; MUIA01000277; OQX35780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1R317; -.
DR   Proteomes; UP000192421; Unassembled WGS sequence.
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; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR43454; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43454:SF1; GP_DH_N DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192421}.
FT   DOMAIN          131..293
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   483 AA;  53248 MW;  5E3CB8B0870C0110 CRC64;
     MTQEKMLDSF ADWKEREAIA EAMIPLVGKL YRDHNVVTSL FGRPIINRSV IDIIKAHRFV
     RQVEQNGLSV RETLPVLEQL ATLKLGPSRI DIGKLAMKFK SQDQFAELND FLRDELKDVL
     GGEQPESENG QDVVLYGFGR IGRLMARILI ERAGGGAGLN LRAIVVRNGG AENDLAKRTS
     LLRRDSVHGS FRGTLSIDEE NQCIIANGVR IQVIYSNSPD SIDYTQYGIN NAIVVDNTGK
     WRDEEGLGLH LKCPGVSRVV LTAPGKGEMK NIVYGVNHNL ISTDDRIVSA ASCTTNAITP
     ILKALLDKFG IANGHVETVH AYTNDQNLID NYHKGDRRGR AAALNMVVTE TGAAKAVAKA
     IPELKGKLTG NAIRVPTPNV SLAILNLNLK SSTTVDELND YLRECSLYSD LQKQIDYVKS
     LEVVSSDFVG SRYAGIVDAE ATIVDGDRCV LYVWYDNEFG YSCQVNRILQ HMAGVMYPVF
     PHS
//
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