ID A0A0F2NYM7_9GAMM Unreviewed; 466 AA.
AC A0A0F2NYM7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=VR73_10185 {ECO:0000313|EMBL:KJS06265.1};
OS Gammaproteobacteria bacterium BRH_c0.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS06265.1, ECO:0000313|Proteomes:UP000033581};
RN [1] {ECO:0000313|EMBL:KJS06265.1, ECO:0000313|Proteomes:UP000033581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS06265.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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}.
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:KJS06265.1}.
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DR EMBL; LADM01000089; KJS06265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2NYM7; -.
DR STRING; 1629722.VR73_10185; -.
DR PATRIC; fig|1629722.3.peg.1042; -.
DR Proteomes; UP000033581; 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}.
FT DOMAIN 113..275
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 466 AA; 51243 MW; AE64B4022CE0F484 CRC64;
MAEGMIPLIG KLYREHNVSL YMYGQNLVNR AVTDIMQAHR YVRQIEHNEL SEFETYPLVK
ALAGMDLGPA HIDIGKLTVL YQEQANGRSV EAFLQEAVGD DIGSTRKPIP QPRDVVLYGF
GRIGRLVARL LIEKTGGGDV LRLRAIVVRK GKSEQDLIKR ASLLRHDSVH GPFTGTIRVI
EEENKLVCNG NVIQVIYANS PQEVDYTAYG IKDAIVVDNT GVWRDEKGLS QHLDCPGASK
VLLTAPGKGS LPNIVYGINH HIIGADDRIV SAASCTTNAI VPVLKVLLDD YGIVKGHVET
VHSYTNDQNL IDNYHKGARR GRSAALNMVL TETGAASAAA KAIPELAGKL TGNSIRVPTP
NVSMAILSLQ LGRDTTVEEI NEFMRQKALY SPLQQQVGYS ISDEAVSTDF VGDRHACVFD
AQATIVNGNT CVLYCWYDNE FGYSCQAVRV LEKMAGVEWA QYPRYF
//
