ID   A0A2A5WG75_9GAMM        Unreviewed;       488 AA.
AC   A0A2A5WG75;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:PDH35333.1};
DE            EC=1.2.1.12 {ECO:0000313|EMBL:PDH35333.1};
GN   ORFNames=CNF02_01050 {ECO:0000313|EMBL:PDH35333.1};
OS   OM182 bacterium MED-G28.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; OMG group; OM182 clade.
OX   NCBI_TaxID=1986256 {ECO:0000313|EMBL:PDH35333.1, ECO:0000313|Proteomes:UP000219329};
RN   [1] {ECO:0000313|EMBL:PDH35333.1, ECO:0000313|Proteomes:UP000219329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED-G28 {ECO:0000313|EMBL:PDH35333.1};
RA   Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA   Rodriguez-Valera F.;
RT   "Fine stratification of microbial communities through a metagenomic profile
RT   of the photic zone.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {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:PDH35333.1}.
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DR   EMBL; NTJZ01000001; PDH35333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5WG75; -.
DR   Proteomes; UP000219329; Unassembled WGS sequence.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; 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   ECO:0000313|EMBL:PDH35333.1}.
FT   DOMAIN          136..297
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   488 AA;  54458 MW;  DB8E14896DB11B8D CRC64;
     MERPSVEDYF ADWKQREALV QEMIPVIGRL FSQRNVGIYI YGRPLHNRSV TFIMKSHRFV
     RQVERNEMSE FETHPVLIAM AKLDLWNAQI DLGKLTVSYM GHLDEQGEGA SSVDDFVRQE
     MTYLDGVNEK PIEKSQDIVL YGFGRIGRLM ARLLIERTST GDVMRLRAIV IRPGEEGDLD
     KRASLFASDS VHGAFQGTLR VDEESKCLVA NGNVIQVIYA NSPEEVNYND YDIDDALVID
     NTGQWRDEEG LSLHLKSKGA AKVILTAPGK GSLKNIVYGI NDDQMSPDDK IITAASCTTN
     AIAPVLKVVN DKFGIEHGHV ETVHAYTNDQ NLIDNYHKGS RRGRSAALNM VLTETGAAKA
     VVKAIPELEG KLTGNAVRVP IPNVSMAIMN LSLSMPTSKV ELNEFLRDIA LHSNLQNQIS
     YTQSPDAVSS DFVGTREAGI VDANATIVRD NHCVLYLWYD NEFGYCCQVA RMVYKMAGVK
     FQVYPQDE
//