ID C5D8H9_GEOSW Unreviewed; 454 AA.
AC C5D8H9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN OrderedLocusNames=GWCH70_3159 {ECO:0000313|EMBL:ACS25817.1};
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS25817.1};
RN [1] {ECO:0000313|EMBL:ACS25817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS25817.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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}.
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DR EMBL; CP001638; ACS25817.1; -; Genomic_DNA.
DR AlphaFoldDB; C5D8H9; -.
DR STRING; 471223.GWCH70_3159; -.
DR KEGG; gwc:GWCH70_3159; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_3_0_9; -.
DR OrthoDB; 9767256at2; -.
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 35..212
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 454 AA; 48797 MW; 416EF1B203160C3A CRC64;
MGLYEDLLER IGDRERVTVN ETVLEQHSKG ISYHAPRKPD VVVFPKTAAE VSAVLSYANE
RRIPVTPFGA GTSLEGHIIP VQGGITINFT MMNNIIDIRP DDFLAIVEPG VTRMQLNQAL
KKHGLFFPVD PGADATIGGM ASTNASGTNS VKYGVMRDQV LGLEVVLADG KIVHTGGMAV
KSSAGYDLTG LFVGSEGTLG VFTKIIVRLQ GIPEATNAIK VSFPTLAEAA QAAASILKAG
VSPGKIELVD EQTIQAVNQY KQTDYPAAPT LFIELSGSAS SVKDGTELVK ELCVAENAVS
FEMEEDSVAR AKLWEARHHA AFAIQAAYPG KAMLSTDVCV PISKMPKAIA ETRKLVDEYG
MTAAILGHVG DGNYHTILAF DPADKEEVKR VEEVNARIVR YALSHGGTCT GEHGIGIGKR
HFLYEEHRDS IPLMKGIKQL FDPNGIMNPG KIFL
//
