ID R8HZ42_BACCE Unreviewed; 463 AA.
AC R8HZ42;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=IIC_00979 {ECO:0000313|EMBL:EOO78027.1};
OS Bacillus cereus VD021.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053224 {ECO:0000313|EMBL:EOO78027.1, ECO:0000313|Proteomes:UP000014040};
RN [1] {ECO:0000313|EMBL:EOO78027.1, ECO:0000313|Proteomes:UP000014040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD021 {ECO:0000313|EMBL:EOO78027.1,
RC ECO:0000313|Proteomes:UP000014040};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD021.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:EOO78027.1}.
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DR EMBL; AHES01000005; EOO78027.1; -; Genomic_DNA.
DR RefSeq; WP_016100874.1; NZ_KB976273.1.
DR AlphaFoldDB; R8HZ42; -.
DR PATRIC; fig|1053224.3.peg.983; -.
DR HOGENOM; CLU_017779_3_0_9; -.
DR Proteomes; UP000014040; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT DOMAIN 39..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 51096 MW; 457307A746CA64D0 CRC64;
MEITIERLVN ELKDVLPEDQ VVVNKTVREL HSKDESYHNS SLPDVVVFPK TMEEVRAIMK
IASEHKKPVI PFGVGSSLEG HIIPYEKGIT VDFSLMNKIL EIREKDFLVK VQPGVTRSQL
NKELKKYGLF FSVDPGADAT LGGMAATNAS GTTAVKYGVM RDQVRDLEVV LADGQVIHTG
NLAAKSSSGY HLNGIFVGSE GTLGCFTELT LKVYGIPEHV MAARASFPTI NDAVEAVINI
LQAGIPIARI ELVDELSMKQ VNHYNETNYR EEPTLFLEFH GNEAGLTQDI EFTKEIVFDH
KCKEVAFETE TAARNKLWDA RHNLAYSYVH SYPGKKLMST DVCVPISELA GAIQNAKETL
DKVGLVGGIL GHVGDGNFHV LLMIDPNDKD EVKKADEINE SIVLYALKRG GTCTGEHGVG
IGKQKYQEEE HGAALLVMEK IKKALDPQNI LNPNKIFKLT DKE
//
