ID A0A1F1UQZ5_9CORY Unreviewed; 488 AA.
AC A0A1F1UQZ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00021022, ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=HMPREF3170_09405 {ECO:0000313|EMBL:OFT28525.1};
OS Corynebacterium sp. HMSC08D02.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581138 {ECO:0000313|EMBL:OFT28525.1, ECO:0000313|Proteomes:UP000177600};
RN [1] {ECO:0000313|EMBL:OFT28525.1, ECO:0000313|Proteomes:UP000177600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08D02 {ECO:0000313|EMBL:OFT28525.1,
RC ECO:0000313|Proteomes:UP000177600};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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:OFT28525.1}.
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DR EMBL; LWNU01000045; OFT28525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F1UQZ5; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000177600; Unassembled WGS sequence.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProt.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; 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:UP000177600}.
FT DOMAIN 130..291
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 488 AA; 53726 MW; BAC8277EB25379EA CRC64;
MTVSTPTNTT HQQDWNHKLT LAQEMLPLIS QLHRENNVVT SIFGRLLVGV TDIDIIKAHR
YARRIVEKEL PLEDTLPVLR ELVQMNLGTA SIDLGRLASD YKKSGASDLR AYLNEALADV
VDTDSELEPR DVVLYGFGRI GRLLARILIA REAMYGGARL RAVVVRKKGD DDIVKRASLL
RRDSVHGPFD GTITVDHEKE VIWANGTPIQ MIYANDPASI DYTEYGINDA IVVDNTGVWR
DEAGLSQHLK SKGVSRVLLT APGKGDIKNI VYGINHADIA DGDQILSAAS CTTNGITPVL
KVINDRYGVV HGHVETVHSY TNDQNLADNF HKGDRRGRAA GLNMVLTETG AAKAVSKALP
EFEGKLTGNA IRVPTPDVSM AVLNLELETE TTKDEVNNFL RKVSTDSNLR QQIDYIQSPE
VVSTDLLGTT HAGVVDGLAT ISAGKHLVLY VWYDNEYGYS HQVVRVVEEI AGVRPRIYPA
RTVPEDLK
//
