ID A0A1W2CG40_9SPHI Unreviewed; 482 AA.
AC A0A1W2CG40;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Glyceraldehyde 3-phosphate dehydrogenase {ECO:0000313|EMBL:SMC84150.1};
GN ORFNames=SAMN04488101_10415 {ECO:0000313|EMBL:SMC84150.1};
OS Pedobacter nyackensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=475255 {ECO:0000313|EMBL:SMC84150.1, ECO:0000313|Proteomes:UP000192678};
RN [1] {ECO:0000313|EMBL:SMC84150.1, ECO:0000313|Proteomes:UP000192678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19625 {ECO:0000313|EMBL:SMC84150.1,
RC ECO:0000313|Proteomes:UP000192678};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWYB01000004; SMC84150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2CG40; -.
DR STRING; 475255.SAMN04488101_10415; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000192678; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD 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 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; IPR036291; NAD(P)-bd_dom_sf.
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 Reference proteome {ECO:0000313|Proteomes:UP000192678}.
FT DOMAIN 130..292
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 482 AA; 53612 MW; 583DC36C17C59F37 CRC64;
MLKKYQSEFQ NWIEKEKKAI ELINIVGQLW FDRSVELVLF RKPLFDVGSS EILAHHQYAK
EVSGKDISIY ETLELATTIA KCNLAPSRVD IGRLASEWLT DNNDYPSMHD FVVNKLSKHI
GKDKISLKPK DVVLFGFGRI GRIAARELIL QAGKGEQLRL RAIVTRSYSD EELIKRGELL
RTDSIHGPFN GTIIEDFENK ALIINGQTVH FIEASSPESV DYTAYDIEDA LLIDNTGIYR
DREGLGRHLK AKGISKVLLT APAKGDIPNV VAGINDSEID FNVENILSNA SCTTNAIVPV
LKIVDDAFGI EKGHIETVHS YTNDQNLLDN YHKKYRRGRS AALNLVITET GADKAVAKVI
PHLGGKLTGN AVRVPTPNVS LAILNLSLNK ITSKEEVSEV LKQASLFGDL SEQIEYSISN
ELVSTDLIGN SHASIIDGPA TIIAKDNKSV VLYTWYDNEY GYTRQVIRLA KKMAGVIRLT
YY
//
