ID R9I3S9_BACUN Unreviewed; 981 AA.
AC R9I3S9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=C801_00845 {ECO:0000313|EMBL:EOS10897.1};
OS Bacteroides uniformis dnLKV2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1235787 {ECO:0000313|EMBL:EOS10897.1, ECO:0000313|Proteomes:UP000014212};
RN [1] {ECO:0000313|EMBL:EOS10897.1, ECO:0000313|Proteomes:UP000014212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dnLKV2 {ECO:0000313|Proteomes:UP000014212};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides uniformis dnLKV2.";
RL Submitted (APR-2013) 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:EOS10897.1}.
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DR EMBL; ASSO01000004; EOS10897.1; -; Genomic_DNA.
DR RefSeq; WP_016272482.1; NZ_KE159482.1.
DR AlphaFoldDB; R9I3S9; -.
DR PATRIC; fig|1235787.3.peg.871; -.
DR HOGENOM; CLU_013688_0_0_10; -.
DR Proteomes; UP000014212; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR009051; Helical_ferredxn.
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; PF02754; CCG; 2.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF13534; Fer4_17; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000014212}.
FT DOMAIN 39..267
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 560..589
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 981 AA; 108890 MW; 6163880F449D979B CRC64;
MKEHSYMAFL QEAKQFIPQE RIYTDELRRL AWGTDAGFYR LIPQIVIRSK DEDEVSQLLK
LASRHGLPVT FRAAGTSLSG QAISDSILIV AGKNWEKYSI SADYEQITLQ PGIIGQRVNE
LLAPYGRKFA PDPASVKSAM VGGIVMNNAS GMNCGTHANS DKVLISARII LMDGTLLDTG
NPVSRASFEV SHRDFIRRIC ELRDEIRTNE KLAERIRYKY SIKNVTGLNL LPFVRFDDPF
EIIAHLMVGS EGTLAFLSEV TMKTEYDYPY KASAMLYFKT IKEASRAVVA MKKLVDETGE
WTVKGAEMLD YKSLSSVNDP VFLKYKGEVA SSALPGVEPG DETGLTAVLT ETKARTPEEL
QQNISAIEAC LQAFTTYIPV RFTDRPEEYS KYWAIRSGIF PSVGGTRQPG TTCLIEDIAF
HIEDLPEATA ELQQLIARHG YNDACIYGHA LEGNYHFIIN QSFSTQAEVK RYEDLMNDIK
TLVVDKYDGS LKAEHGTGRN MAPFVCHEWG DDAYKAMKAV KELFDPQGLL NPGVIFNDDP
QCHIKNFKPL PLLVMSDKRQ ATSLVADKCI ECGFCEVNCL SCGFTLSSRQ RIVLQREISR
LKQSGEDPTR LALLEKQYRY PGNQTCAGDG LCSMSCPMGI NTGDLTHIIR QEALPKGSLG
YKAGDFVANH FAGVKSALRP VLSLANFGHS LLGTKAMSGI TKGLHNALGI PLWTPAMPKS
YQLQATSTMQ HNSAALVARS SVTRNYKVVY FPSCINQTMG LAKKSPVEQP LVNKMVSLLQ
KAGYEIIFPK DMDKLCCGTI WESKGMLDIA DRKTAELEAA LWEASEQGKY PVLCDQSPCL
HRMRECIKKM KLYEPAEFIY TFLREKLIFT PINRPVAIHI TCSMRKMGLA DTIIALARLC
SSKVIVPEEV GCCGFAGDRG FTYPELNSYA LRKLRPQIEA SGVNIGYSNS RTCEIGLTTN
SGIPYVSIAY LVDECTKAAD N
//
