ID A0A101HYD2_9BACT Unreviewed; 352 AA.
AC A0A101HYD2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KUK84435.1};
DE Flags: Fragment;
GN ORFNames=XE01_1414 {ECO:0000313|EMBL:KUK84435.1};
OS Synergistales bacterium 58_81.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635274 {ECO:0000313|EMBL:KUK84435.1, ECO:0000313|Proteomes:UP000054873};
RN [1] {ECO:0000313|Proteomes:UP000054873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001878};
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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:KUK84435.1}.
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DR EMBL; LGGV01000140; KUK84435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101HYD2; -.
DR STRING; 1635274.XE01_1414; -.
DR PATRIC; fig|1635274.3.peg.303; -.
DR Proteomes; UP000054873; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR CDD; cd04902; ACT_3PGDH-xct; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR029009; ASB_dom_sf.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR045626; PGDH_ASB_dom.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF19304; PGDH_inter; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 276..352
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK84435.1"
SQ SEQUENCE 352 AA; 37818 MW; EF9ED2218A0FD3F7 CRC64;
ADIVTLHVPL TRETHGMIDA KTMKACKRGA FIVNCARGGL VDENACAEAV RSGHLSGAAF
DVFDGEPVRQ DHPLFAEDIR DRIVLTPHIG ANTEEAQSAV ATIACSNLLA ALKGKPCENA
VNLPFVEQTL SDGSRAFLSL ARKLGFLAAH LVREPVKNIR IALRGPLFSP GDDPICFEIP
YHYSPFSVAG LKGFLEYSHG PEVNYMSAPL IAADKGIRVE EARTSGGTWK NQIDLSLSVE
EQRETVTVSG TVTEEGRQRV VNICGYWIEF IPEGTVLLFS NHDRPGVIGK VGTLLGKAGA
NIANFALGRK NGSGLAVGAL QIDDDISGAI VETMKEDVDL LWAEKINFAE AL
//