ID A0A0M3V976_9GAMM Unreviewed; 481 AA.
AC A0A0M3V976;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=AOC03_10780 {ECO:0000313|EMBL:ALF60463.1};
OS Psychrobacter urativorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=45610 {ECO:0000313|EMBL:ALF60463.1, ECO:0000313|Proteomes:UP000059847};
RN [1] {ECO:0000313|EMBL:ALF60463.1, ECO:0000313|Proteomes:UP000059847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R10.10B {ECO:0000313|EMBL:ALF60463.1,
RC ECO:0000313|Proteomes:UP000059847};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Psychrobacter urativorans R10.10B.";
RL Submitted (SEP-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; CP012678; ALF60463.1; -; Genomic_DNA.
DR RefSeq; WP_062535891.1; NZ_CP012678.1.
DR AlphaFoldDB; A0A0M3V976; -.
DR STRING; 45610.AOC03_10780; -.
DR KEGG; pur:AOC03_10780; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000059847; 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; 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 131..291
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 481 AA; 51621 MW; 415FFA9E046B0333 CRC64;
MFLVSNADTL RQLHQDHLSQ YNNQEQQAIE LIGLLNKLYN EQDVQVTLFG ETLDSTSVSR
VLALHQKAAI RESGAEPIAI ADTLDMVKAI AAHTNIQSAS IDVGQLIVNN SDLEAALQAV
NTSEQAQNGA TDVVLYGFGR IGRILTRLLL SKASSAKGLQ LKAIVVRPAK AGDLAKRVSL
LERDSIHGSF TGGVSIDDDN NGMIINGRFV QVIYANDPSE IDYTAYGIDN ALVIDNTGIW
KDEDGLGKHL HSKGVKKVLL TAPAGGEIKN VVYGVNNNTV GDDTIVSAAS CTTNAITPML
KVLNDEFGIE NGHVETIHSF TNDQNLIDNY HKADRRGRSA VLNMVITSTG AAKAVGKALP
ELSGKLTGNA IRVPTPNVSL AILNLNLKTA PASADALNDF MRKVSNSNQW QSQIAYTDST
EAVSTDFVGD THVGVVDAQA TILTDNHAIV YIWYDNEVGY STQVLRLATQ MAGISYTQVP
A
//
