ID F2B1N9_RHOBT Unreviewed; 359 AA.
AC F2B1N9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:EGF24166.1};
GN ORFNames=RBWH47_05425 {ECO:0000313|EMBL:EGF24166.1};
OS Rhodopirellula baltica WH47.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF24166.1, ECO:0000313|Proteomes:UP000006222};
RN [1] {ECO:0000313|EMBL:EGF24166.1, ECO:0000313|Proteomes:UP000006222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH47 {ECO:0000313|EMBL:EGF24166.1,
RC ECO:0000313|Proteomes:UP000006222};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:EGF24166.1}.
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DR EMBL; AFAR01000307; EGF24166.1; -; Genomic_DNA.
DR RefSeq; WP_007329799.1; NZ_AFAR01000307.1.
DR AlphaFoldDB; F2B1N9; -.
DR PATRIC; fig|991778.3.peg.6244; -.
DR Proteomes; UP000006222; 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; cd05300; 2-Hacid_dh_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 133..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 359 AA; 39338 MW; 3F9DBAE579712F2F CRC64;
MSQPRERLPL SEIDSVRRVV LCYPALPRHI EQLETTLAEL KADPNCKLNH DVEVVDAGQE
RIDELLPTAD IFIGHAKVPV DWDRVLAAGR LGWIQSSAAG LDHCLVPGVI ANPNIMVSSA
SGLFAPQVAE QTFALLFGVL RRIGLFERAR PKREFIRLPT DDLRGKTIGI VGLGGNGRAI
AAKLAPWDVR LIATDYYPED CPTEVETLWP ADRVNDLFAA SDIVILTLPL NASTRKWIGA
EQIAAMKPGG YLINVARGQV LDEEALIDAL QSGHLAGAGV DVTYTEPLPE DSPLWDDPNV
LITPHVGAQS ARRVDDSNDL ACVNLRRYFH GETIINRVDK TLGFPHPNDS HAAWVQSRS
//
