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Database: UniProt
Entry: A0A1U7DL59_9RHOB
LinkDB: A0A1U7DL59_9RHOB
Original site: A0A1U7DL59_9RHOB 
ID   A0A1U7DL59_9RHOB        Unreviewed;       334 AA.
AC   A0A1U7DL59; A0A2M9DBF3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glyceraldehyde 3-phosphate dehydrogenase {ECO:0000313|EMBL:PJJ85122.1};
DE   SubName: Full=Type I glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:APX90720.1};
GN   ORFNames=BV394_14180 {ECO:0000313|EMBL:APX90720.1}, CLV77_1983
GN   {ECO:0000313|EMBL:PJJ85122.1};
OS   Brevirhabdus pacifica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Brevirhabdus.
OX   NCBI_TaxID=1267768 {ECO:0000313|EMBL:APX90720.1, ECO:0000313|Proteomes:UP000187266};
RN   [1] {ECO:0000313|EMBL:APX90720.1, ECO:0000313|Proteomes:UP000187266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY6-4 {ECO:0000313|EMBL:APX90720.1,
RC   ECO:0000313|Proteomes:UP000187266};
RA   Wang X.;
RT   "Genomic analysis of Xuhuaishuia manganoxidans DY6-4.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PJJ85122.1, ECO:0000313|Proteomes:UP000229573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27767 {ECO:0000313|EMBL:PJJ85122.1,
RC   ECO:0000313|Proteomes:UP000229573};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) 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; CP019124; APX90720.1; -; Genomic_DNA.
DR   EMBL; PGFI01000012; PJJ85122.1; -; Genomic_DNA.
DR   RefSeq; WP_076980737.1; NZ_PGFI01000012.1.
DR   AlphaFoldDB; A0A1U7DL59; -.
DR   STRING; 1267768.BV394_14180; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000187266; Chromosome.
DR   Proteomes; UP000229573; 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; 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; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR   PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187266}.
FT   DOMAIN          3..151
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        151
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         12..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         150..152
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         181
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         209..210
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         232
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            178
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ   SEQUENCE   334 AA;  35836 MW;  36DA4989456609F9 CRC64;
     MTTTIGINGF GRIGRCTLAH IAESARNDVQ VVKINATGPV ETNAHLLKYD SVHGRFGGEV
     RVSGNTMDLG RGPMEMFSTY DPNELDWSGC DIVLECTGKF NDGKKSAVHL DRGAKAVLIS
     APATNVDRTV VYGVNHREMQ PGERMISNGS CTTNCLAPLA KVLHEGIGIE NGLMTTIHSY
     TGDQPTLDRR HADLYRARAA ALAMIPTSTG AAKALGEVLP DLKGKLDGTA IRVPTPNVSA
     VDLTFNAKRD VTVEEVNALM QEAAAGHMGA VLAYDAEPKV SIDFNHTSHS SIFAPDQTKV
     LGGRLVRVLA WYDNEWAFSC RMADTAAAMG RLLN
//
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