ID A6FDZ6_9GAMM Unreviewed; 475 AA.
AC A6FDZ6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 13-SEP-2023, entry version 66.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=PE36_04178 {ECO:0000313|EMBL:EDM66599.1};
OS Moritella sp. PE36.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM66599.1, ECO:0000313|Proteomes:UP000004278};
RN [1] {ECO:0000313|EMBL:EDM66599.1, ECO:0000313|Proteomes:UP000004278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE36 {ECO:0000313|EMBL:EDM66599.1,
RC ECO:0000313|Proteomes:UP000004278};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM66599.1}.
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DR EMBL; ABCQ01000023; EDM66599.1; -; Genomic_DNA.
DR RefSeq; WP_006032605.1; NZ_ABCQ01000023.1.
DR AlphaFoldDB; A6FDZ6; -.
DR STRING; 58051.PE36_04178; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000004278; 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 127..287
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 475 AA; 52386 MW; 16C54D9D461E50FA CRC64;
MPSESHLLNW QESQELAESM LPLLGKLYRN KGVEVLIYGR PLQNATAIDL QKAHRVVKRH
EGRVLRFTET FPLLQIISEL PISNSQIDIG RLAVRYWADN EDSTGIDAFL RAELAPALNN
DTQPEPRDVV LYGFGRIGRL LARLLVDKTG ESNLLRLRAI VVRGGPGDIE KRASLLRRDS
VHGQFNGTID IDEENNAIIA NGTYIKILYS NGPDQIDYEA HGIHNALIVD NTGIWRDTDG
LGLHLKAPGA AKVLLTAPGK GDIKNIVYGV NHMDILPEDN IVSAASCTTN AITPVLKTIQ
DRYGIENGHV ETVHSYTNDQ NLIDNYHKGD RRGRGAAMNM VLTSTGAASA VAKALPELKG
KLTGNAIRVP TPNVSMAIIN LNLEKEVERE SLNSYLQEMS LSSPLHNQID FSTSKELVST
DMVGSRFSGI VDSLATIAQG NRAILYVWYD NEFGYSCQVL RVMQKMAGIN MHEFA
//
