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Database: UniProt
Entry: A0A1M4ZUK3_9BACE
LinkDB: A0A1M4ZUK3_9BACE
Original site: A0A1M4ZUK3_9BACE 
ID   A0A1M4ZUK3_9BACE        Unreviewed;       933 AA.
AC   A0A1M4ZUK3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=SAMN05444405_10657 {ECO:0000313|EMBL:SHF21625.1};
OS   Bacteroides luti.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHF21625.1, ECO:0000313|Proteomes:UP000184509};
RN   [1] {ECO:0000313|EMBL:SHF21625.1, ECO:0000313|Proteomes:UP000184509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26991 {ECO:0000313|EMBL:SHF21625.1,
RC   ECO:0000313|Proteomes:UP000184509};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQTV01000006; SHF21625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M4ZUK3; -.
DR   STRING; 1297750.SAMN05444405_10657; -.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000184509; 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:UP000184509}.
FT   DOMAIN          38..266
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          521..552
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   933 AA;  103983 MW;  B53C86F491B4E003 CRC64;
     MSKNYNSLLE EISAFVPKDR IYTDELRLLA WGTDAGFYRL IPKIVIRSVD EQEISRILLI
     ADSLNLPVTF RAAGTSLSGQ SISDSILIVA GKHWEKYTIS PDYKTITLQP GLIGERVNQI
     LKPFGRKFAP DPASVKSAMV GGIIMNNASG MNCGTHANSD KMLLSVRIVM ADGTILDTGN
     ENSKRNFAKK KPDFIKGIEA LRDKIRNDEK LSERIRYKYS IKNVTGLNIL PFVEHDDPFE
     IITHLMVGSE GTLAFLSEAT MRTGYDYPFS ASAMLYFKDI KEACRAVVAM KKGPVMGAEL
     LDSKSLSSVN DPTGEGLTAV LTETKAATKQ ELDDQIKEIE TILESFETYT PVHFTDKESE
     YSKYWNIRSG IFPSVGGTRE LGTTTLIEDV AFHIENLPEA TAELQALLVK HGYADACIYG
     HALEGNYHFI INQAFDTDEK VRKYENLMNE VKTLVVDKYD GSLKAEHGTG RNMAPFVKYE
     WGEAAFEVMK EVKNLFDPKN LINPGVIFND DPECHIKNFK PLPLTNAHVD KCIECGFCEV
     NCLTCGFTLS SRQRIVIRRE ISRLRKSGED NERLAKLEQQ YKYLGNQTCA GDGLCSMSCP
     MNINVGDLTH DIRQEELPVG SLGYKIGDFA ANHFQGMKSI LRPVLSLANG AHSVLGTKTM
     TSLTKGIRYV SMDNFPLWTP AMPKAYYPHK ITQKSEPLKV VYFPSCLNQM MGTAKETPDA
     TPLVDKTVQL LQKAGYEVIF PKDMDKLCCG TIWESKGMMD IADRKSAELE EALFAATEQG
     KYPVLCDQSP CLHRMRNVMT KVKLYEPVEF IYTFLKDKLD FTPIDKPVSI HITCSTQKMG
     LRDQMVALAS LCSTKVIVPE EVGCCGFAGD KGFTHPEVNT YALRKLKPQL EKAGVEVGYS
     NSRTCEIGLT TNSGIPYISI VYLVDQCTTA ITK
//
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