ID C1A6T4_GEMAT Unreviewed; 345 AA.
AC C1A6T4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:BAH37944.1};
GN OrderedLocusNames=GAU_0902 {ECO:0000313|EMBL:BAH37944.1};
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH37944.1, ECO:0000313|Proteomes:UP000002209};
RN [1] {ECO:0000313|Proteomes:UP000002209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC {ECO:0000313|Proteomes:UP000002209};
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP009153; BAH37944.1; -; Genomic_DNA.
DR AlphaFoldDB; C1A6T4; -.
DR STRING; 379066.GAU_0902; -.
DR KEGG; gau:GAU_0902; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_0; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000002209; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002209}.
FT DOMAIN 127..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 345 AA; 36667 MW; 0ADC4E566B0E2E9A CRC64;
MTMRRLVVDM QSSAPHMRLP AWAADEITAN TPDGWEVAHI ATQSRSLGNG TNEPSAETLA
AIPAAEAYFG YGLTPPLLAA APGLRWAHSA SAGIGESITP ELRESRVVFT NGAGIYAEPM
ADTVLGGVLH FVRGLDLAVR LQAASIWDRH PFVDNNGGIR ELSEYRVLVI GAGGIGSAVA
QRLQALGCTC IGVRRRPALG IPAGFTRVVG PDALEEVLPL GDITVVAAPL TDGTRSLLDG
GRMALLPAGA IVVNVARGPL VDDAALLEGL ESGRLRGAVL DVFSTEPLPA DSPWWQHPRV
LVTPHVSGVS PRRTWQRGIA LFMDNWRRWS AGERLHNVVD LDAGY
//
