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
//