ID K4IMB1_BIFAP Unreviewed; 330 AA.
AC K4IMB1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:AFU71489.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:AFU71489.1};
GN OrderedLocusNames=BAST_0909 {ECO:0000313|EMBL:AFU71489.1};
OS Bifidobacterium asteroides (strain PRL2011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU71489.1, ECO:0000313|Proteomes:UP000007006};
RN [1] {ECO:0000313|EMBL:AFU71489.1, ECO:0000313|Proteomes:UP000007006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU71489.1,
RC ECO:0000313|Proteomes:UP000007006};
RX PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA Ventura M.;
RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT colonization of the insect gut.";
RL PLoS ONE 7:E44229-E44229(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP003325; AFU71489.1; -; Genomic_DNA.
DR RefSeq; WP_015021928.1; NC_018720.1.
DR AlphaFoldDB; K4IMB1; -.
DR STRING; 1147128.BAST_0909; -.
DR GeneID; 41010156; -.
DR KEGG; bast:BAST_0909; -.
DR PATRIC; fig|1147128.3.peg.924; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_11; -.
DR Proteomes; UP000007006; Chromosome.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12186; LDH; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 35821 MW; 17811E46E1A123EB CRC64;
MTSILMYSVR PDEQEAIQAW AQANDIQVDT TDHDLGMKTV DMIKGYDGIV IQQHAALPEP
ELYQRLREYG LKQLTLRITG YDIVNLQAAR ENGLVVTNVP AYSPRSVSEL VLAQVMRLVR
HLGEASAREA KDDYTWAGLQ AHEIHNLTVG IIGAGKIGSA VARIFRALGS TVIANDPIHR
PELADTLDYV DLPILLKRAD IVTVHTPLDE TTHHLINAQA LEAMKPSAFL INAARGPIVD
TPALIKALQT KSIAGAAIDT IEGEAGIFEN DLSGTKVDNQ ALETLKAMPN VEVSPHIGFY
TDAAVTAMVN ISLNDVKTIL EGGTSEHQVD
//
