ID A0A2V3ZX06_9BACT Unreviewed; 314 AA.
AC A0A2V3ZX06;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:PXX97106.1};
GN ORFNames=DF185_18985 {ECO:0000313|EMBL:PXX97106.1};
OS Marinifilum breve.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae.
OX NCBI_TaxID=2184082 {ECO:0000313|EMBL:PXX97106.1, ECO:0000313|Proteomes:UP000248079};
RN [1] {ECO:0000313|EMBL:PXX97106.1, ECO:0000313|Proteomes:UP000248079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC075 {ECO:0000313|EMBL:PXX97106.1,
RC ECO:0000313|Proteomes:UP000248079};
RA Fu T.;
RT "Marinifilum breve JC075T sp. nov., a marine bacterium isolated from Yongle
RT Blue Hole in the South China Sea.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:PXX97106.1}.
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DR EMBL; QFLI01000010; PXX97106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3ZX06; -.
DR OrthoDB; 9777288at2; -.
DR Proteomes; UP000248079; 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 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 22..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 314 AA; 34519 MW; A3C234BC8B0494D9 CRC64;
MKFTILEPIG MTACKYGQLK KEFEELGHEL VFFGDRNEDE QELIKRAEGA DAIVVSNIPI
TKNFINACPN LSMISVAFTG VDHIDMQACN ERNILVSNAA GFSNESVAEL AIGMILSVYR
KIVGGDAMTR FGGDRGGFLG TELNGKTLGI IGAGEIGLRV AEIAKVFNCN VLAYSRSEKS
VEGVKFVDKE TLLKESDIVS LHVPLTSETK GLMGKDEFKL MKPEAILINT ARGPVVDSDA
LCWALDEHEI AGAAVDVYEK EPPLDKEHIL FTAPNLIMLP HIAYATNESF EKRIDIVMEN
IKLWLQGKPR NIMN
//
