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Database: UniProt
Entry: A0A063Y6T4_9GAMM
LinkDB: A0A063Y6T4_9GAMM
Original site: A0A063Y6T4_9GAMM 
ID   A0A063Y6T4_9GAMM        Unreviewed;       339 AA.
AC   A0A063Y6T4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=D-erythrose-4-phosphate dehydrogenase {ECO:0000313|EMBL:KDE40147.1};
DE            EC=1.2.1.72 {ECO:0000313|EMBL:KDE40147.1};
GN   ORFNames=ADINL_0739 {ECO:0000313|EMBL:KDE40147.1};
OS   Nitrincola lacisaponensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE40147.1, ECO:0000313|Proteomes:UP000027318};
RN   [1] {ECO:0000313|EMBL:KDE40147.1, ECO:0000313|Proteomes:UP000027318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4CA {ECO:0000313|EMBL:KDE40147.1,
RC   ECO:0000313|Proteomes:UP000027318};
RX   PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA   Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA   Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT   "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT   bacterium isolated from an alkaline, saline lake.";
RL   Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
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:KDE40147.1}.
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DR   EMBL; JMSZ01000016; KDE40147.1; -; Genomic_DNA.
DR   RefSeq; WP_036544107.1; NZ_JMSZ01000016.1.
DR   AlphaFoldDB; A0A063Y6T4; -.
DR   STRING; 267850.ADINL_0739; -.
DR   PATRIC; fig|267850.7.peg.733; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000027318; Unassembled WGS sequence.
DR   GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase 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; PTHR43148:SF3; D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43148; 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.
DR   PROSITE; PS00071; GAPDH; 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   ECO:0000313|EMBL:KDE40147.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027318}.
FT   DOMAIN          3..155
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        155
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         123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         320
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            182
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ   SEQUENCE   339 AA;  37584 MW;  11C0BD247080CEF9 CRC64;
     MSYRIAINGY GRIGQSVLRA LYERGLQKRL QVVALNELSD IETLTYLTRY DTTHGRFPLP
     VSHDGEQLLI DGDAIRVLSV EDPEFLPWTA LDVDLVLDCS GSFSDRAQAH KHLNSGAKRL
     LFSNPASADI DATIIYGINH SQLNATQRIV SAASCTTNCL VPVLELLDRH FGIVNGVTTT
     VHSAMNDQPV IDSYHRTDLR LTRSALQSII PVDTGLSKGI DRLLPHLAGR FQCLHLRVPT
     INVSLMDLSV NLAVDVSVEE VNTLMRQSAV EGALVNLLGY TEEPHASVDF NRDGRSVIVD
     GTQTRVSGGR LLKLICWFDN EWGYANRMLD VAEHWLEQT
//
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