ID A0A1G2FFW4_9BACT Unreviewed; 319 AA.
AC A0A1G2FFW4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:OGZ36707.1};
GN ORFNames=A3J64_00315 {ECO:0000313|EMBL:OGZ36707.1};
OS Candidatus Portnoybacteria bacterium RIFCSPHIGHO2_12_FULL_38_9.
OC Bacteria; Candidatus Portnoybacteria.
OX NCBI_TaxID=1801997 {ECO:0000313|EMBL:OGZ36707.1, ECO:0000313|Proteomes:UP000177061};
RN [1] {ECO:0000313|EMBL:OGZ36707.1, ECO:0000313|Proteomes:UP000177061}
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:OGZ36707.1}.
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DR EMBL; MHNB01000023; OGZ36707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2FFW4; -.
DR STRING; 1801997.A3J64_00315; -.
DR Proteomes; UP000177061; 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 GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd05301; GDH; 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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 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 4..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 35209 MW; D3C5B64E76B5B5A6 CRC64;
MPKIFITREI PENGINLLKE KGWEVGVGPE EIISQEELLE GVKGADAILS VLTEKIDREV
MEAAGPQLKI IANYAVGYDN IDIAEAKKRG ISATNTPGVL TEAVAEHTIA LLLAAACRIA
EGDRYTRAKK FKGWGPKLFL GADIHGKTLA IIGLGRIGSE VARRMRDGFD LKIIYYDIRR
NEELEKKYNI EYREIDALLK EADFISLHTA LTPETRHLIS AERLKMMKPT SYLINTSRGP
IIDEKALVEA LKNKTIAGAA LDVFENEPEL TPGLTELENV VLTPHIASAT KETRDKMSEM
AAQNIIAALE GRTPPNLVK
//
