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Database: UniProt
Entry: B9Z038_9NEIS
LinkDB: B9Z038_9NEIS
Original site: B9Z038_9NEIS 
ID   B9Z038_9NEIS            Unreviewed;       338 AA.
AC   B9Z038;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:EEG09921.1};
GN   ORFNames=FuraDRAFT_0937 {ECO:0000313|EMBL:EEG09921.1};
OS   Pseudogulbenkiania ferrooxidans 2002.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Pseudogulbenkiania.
OX   NCBI_TaxID=279714 {ECO:0000313|EMBL:EEG09921.1, ECO:0000313|Proteomes:UP000003165};
RN   [1] {ECO:0000313|EMBL:EEG09921.1, ECO:0000313|Proteomes:UP000003165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002 {ECO:0000313|EMBL:EEG09921.1,
RC   ECO:0000313|Proteomes:UP000003165};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Coates J.D.;
RT   "Sequencing of the draft genome and assembly of Lutiella nitroferrum
RT   2002.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:EEG09921.1}.
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DR   EMBL; ACIS01000002; EEG09921.1; -; Genomic_DNA.
DR   RefSeq; WP_008952957.1; NZ_ACIS01000002.1.
DR   AlphaFoldDB; B9Z038; -.
DR   eggNOG; COG0111; Bacteria.
DR   Proteomes; UP000003165; 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; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          40..333
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          142..316
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   338 AA;  35308 MW;  C02C42272ADD68D6 CRC64;
     MSAGKFETVL PDEPVFWDVE QRPSRQSETE AILPVEHVRV LVCDPIPSVA VERMREGGLL
     VDEWIGLSPA MLEELIGDYD AVVVRSATRL GAQQLAAAQR LRLIVRAGVG TDNIDLAAAA
     SQGIAVLNTP KASTGSVAEL ALGMLLALAR RIPQADAAVK SGGWPKKEFS DGIELAGKTL
     GIIGVGRIGG ALGRCAAALG MVVVGADKAA EPVGRFEGLA LLSLEALLAC ADFVSIHTPP
     SKAGRAVIGK KEIARMKDGV LLVNCARGGL VDEEALLTAL DSGKVRGAAL DVFAGEPPSD
     LRLARHPHVI CTPHLGASTR EAQARIGVEI AQLMLEQL
//
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