ID A0A1F7U3Q4_9BACT Unreviewed; 315 AA.
AC A0A1F7U3Q4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3D72_01040 {ECO:0000313|EMBL:OGL72404.1};
OS Candidatus Uhrbacteria bacterium RIFCSPHIGHO2_02_FULL_57_19.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802391 {ECO:0000313|EMBL:OGL72404.1, ECO:0000313|Proteomes:UP000176303};
RN [1] {ECO:0000313|EMBL:OGL72404.1, ECO:0000313|Proteomes:UP000176303}
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:OGL72404.1}.
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DR EMBL; MGDZ01000064; OGL72404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7U3Q4; -.
DR STRING; 1802391.A3D72_01040; -.
DR Proteomes; UP000176303; 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 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; PS00670; D_2_HYDROXYACID_DH_2; 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 11..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 34273 MW; 1A35258205EE5D59 CRC64;
MRTIIVEPEH YAQEAVDIYR SFGDVLMERA LSRQELLEAI SDAEILVIRL AHKIDREVLK
AAPNLKIIVC PTTGLDHIDL AAAAERGVKV VSLKGETEFL RTIHATAEHT FALLLALLRR
IPWSFASVGR GEWDRDSFKG NELSGKTMGI IGFGRLGSRV ARIAQGFDMS VVATDPLVKI
ETPNVQQVGL PELVSASDVI SIHVPYSSDT ERMISSDIFV RIRQGAVLVN TSRGQVVDEG
ALLGALTSGK LAGAALDVLW AEEKRPVVIS GDPLVEYAKT HQNLLITPHL GGATFESMAK
TEIFIAEKVK AAFTV
//
