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Database: UniProt
Entry: I2B835_SHIBC
LinkDB: I2B835_SHIBC
Original site: I2B835_SHIBC 
ID   I2B835_SHIBC            Unreviewed;       317 AA.
AC   I2B835; K6WEN7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Putative D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:AFJ46689.1};
GN   OrderedLocusNames=EBL_c15950 {ECO:0000313|EMBL:AFJ46689.1};
OS   Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS   CDC 9005-74) (Escherichia blattae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shimwellia.
OX   NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ46689.1, ECO:0000313|Proteomes:UP000001955};
RN   [1] {ECO:0000313|EMBL:AFJ46689.1, ECO:0000313|Proteomes:UP000001955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC   {ECO:0000313|Proteomes:UP000001955};
RX   PubMed=22843577; DOI=10.1128/JB.00829-12;
RA   Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT   "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT   DSM 4481, isolated from a cockroach.";
RL   J. Bacteriol. 194:4436-4436(2012).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP001560; AFJ46689.1; -; Genomic_DNA.
DR   RefSeq; WP_002440161.1; NZ_BAHA01000004.1.
DR   AlphaFoldDB; I2B835; -.
DR   STRING; 630626.EBL_c15950; -.
DR   KEGG; ebt:EBL_c15950; -.
DR   PATRIC; fig|630626.3.peg.1538; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_6; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000001955; Chromosome.
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; cd12156; HPPR; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001955}.
FT   DOMAIN          12..317
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          115..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   317 AA;  34260 MW;  97CB3D52973E6534 CRC64;
     MIQNIATTRP HILLTQPLPE PVEKILLRDY EVHRLYLAHD ANSMLSDIAP LIQGVVTGGA
     KGFSRELMAQ LPALKIVAIS GIGTDAVDLA YAARRGIYVT TTPDILTDDV ADMAMGLIIA
     TLRRMSEAEH IVRTGQWPGS TLPLARKVSG ATLGIIGLGR VGQAIARRAV AFSMPVRYTS
     LTPCEHVDYT FVEDVHELAR QVDVLVLAAS ADSGQVIVSD TVIEALGPDG YFINVARGKL
     VDEAALLDAL IHRRIAGAGL DVFAREPHVP EAFFTLPNVT LQPHRASATT QTRIEMGMRV
     LENLAACFNG QQPPHRV
//
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