ID A0A1F8NVV8_9CHLR Unreviewed; 332 AA.
AC A0A1F8NVV8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phosphoglycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Y93_11390 {ECO:0000313|EMBL:OGO14994.1};
OS Chloroflexi bacterium RBG_13_68_17.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797638 {ECO:0000313|EMBL:OGO14994.1, ECO:0000313|Proteomes:UP000178211};
RN [1] {ECO:0000313|EMBL:OGO14994.1, ECO:0000313|Proteomes:UP000178211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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:OGO14994.1}.
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DR EMBL; MGNF01000054; OGO14994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8NVV8; -.
DR Proteomes; UP000178211; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12172; PGDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 23..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 118..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 35181 MW; 2EE35D36C306A1D5 CRC64;
MSGSAARGKI LVTARSFRKV PGPHQQLLKD AGYELLESPH DRPLEPGELA SLLPGVDGVI
LGVDAVPAAV LEHADRLKVL SRCGVGVDGI DLQAATARGI VVTTTPGANS LAVAELTIAL
MLALLRHIPH HDMVVRQGGW ERRMGSELAG STLGLVGLGR IGREVARRAH VFDMRLLFAD
PDPPPEEAVR SLGADPRDLP SLLSESDIVS LHLPLNGQTQ GIIGVRELEC MKVSGILVNT
SRGGLVDEQA LYAALSQGRL AGAACDVFSE EPPRRSPLLK LDNFIATPHI GSNTLQTALR
MGLMASRNAL TVLEGGRPEH VANPEVYAAK ND
//
