ID A0A1A7QMP2_9SPHN Unreviewed; 312 AA.
AC A0A1A7QMP2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:OBX20726.1};
GN ORFNames=A9995_03285 {ECO:0000313|EMBL:OBX20726.1};
OS Erythrobacter sp. QSSC1-22B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1860125 {ECO:0000313|EMBL:OBX20726.1, ECO:0000313|Proteomes:UP000092728};
RN [1] {ECO:0000313|EMBL:OBX20726.1, ECO:0000313|Proteomes:UP000092728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSSC1-22B {ECO:0000313|EMBL:OBX20726.1,
RC ECO:0000313|Proteomes:UP000092728};
RA Bowman J.P.;
RT "Draft genome of Erythrobacter sp. QSSC1-22B.";
RL Submitted (JUN-2016) 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:OBX20726.1}.
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DR EMBL; LZRP01000001; OBX20726.1; -; Genomic_DNA.
DR RefSeq; WP_067609050.1; NZ_LZRP01000001.1.
DR AlphaFoldDB; A0A1A7QMP2; -.
DR STRING; 1860125.A9995_03285; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000092728; 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; cd05300; 2-Hacid_dh_1; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092728}.
FT DOMAIN 27..301
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 104..274
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 34598 MW; B24810108407F6ED CRC64;
MTTAVLSAMI RPLVEPRLPD WVEPHWFATQ EEALELAPRA EIGWFDFTQH APMIATVEAA
TNLKWLNSIY AGLDFLPLDL LAQRGTVVTN GAGINALTIA EYVVMLMLAH AKGYAEVVRA
MDRHEWLLDS PGKRELAGER VLLLGMGAIG ALVKTRLEAF AMEVVPVRRS GADGALKPDE
WRARLGEFDW VVLAVPSTPE TRHMIGSEEL AAMKSTAVLV NVARGDVVDQ PALIEALRSK
SIEGALLDVT EPEPLPEEHP LWELENAQIT MHLSGRAQTK MFQRSADRFI ANLERWKQGE
PVEPQLDLEL GY
//
