ID A0A0K1RCD4_9CORY Unreviewed; 938 AA.
AC A0A0K1RCD4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=AK829_06300 {ECO:0000313|EMBL:AKV58846.1};
OS Corynebacterium riegelii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156976 {ECO:0000313|EMBL:AKV58846.1, ECO:0000313|Proteomes:UP000060016};
RN [1] {ECO:0000313|EMBL:AKV58846.1, ECO:0000313|Proteomes:UP000060016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PUDD_83A45 {ECO:0000313|EMBL:AKV58846.1,
RC ECO:0000313|Proteomes:UP000060016};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) 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; CP012342; AKV58846.1; -; Genomic_DNA.
DR RefSeq; WP_052205095.1; NZ_CP012342.1.
DR AlphaFoldDB; A0A0K1RCD4; -.
DR STRING; 156976.AK829_06300; -.
DR PATRIC; fig|156976.3.peg.1253; -.
DR Proteomes; UP000060016; Chromosome.
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:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; 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; PF13183; Fer4_8; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000060016}.
FT DOMAIN 39..267
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 531..562
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 938 AA; 100838 MW; F5AC48B950B58514 CRC64;
MTATISNPAA HLARELGSDQ QLSTRPIDRI KYAHDASHFL YMPDVVVGAR NANDVAAAFR
ASASSGAPVV LRAGGTSLSG QAGGGGMLVD VRKHFRGVEV LDGGKRVRVQ PGSTVRQVNA
HLAAYGRKIG PDPASEGAAT IGGVIANNSS GMACGTQFNT YNTIESLTFV LPSGTVINTA
DTDSEAQFAQ QEPELVETLE RLKRRVRGNK ESVDIIQRHF ALKNTMGYSL NSFLDFESPL
DIFMHLLVAS EGTLAFIAEA VFRTIEVPKL KTTTIAVYPT LDAATRSLPA LFDSKAATLE
LMDSRSIKVG RTFDSVPEQI TGFELGGQAA LLIEYHANEL EQLREYEQAG SRLLKEFELQ
TPAQFSTDPL EGAKAWAFRK GLYAQVAEAR PSGTTALLED IAVPVQDLAD TCGGLQQLFD
TYGYDEAVIF GHAKDGNIHF LITDRFEGDE NLKRYDGFNE DMVDLVLGAG GNLKAEHGTG
RVMAPYVRRQ YGDELYEVMV ELKRAADPRG VMNPGVIITE DDREHMKNFK LNPQVEDEID
PCVECGYCEP VCPSRDLTMT PRQRIVVRRA RAKALKEGDM ELVAHIDKEY QYEGIDTCAV
DSMCVTACPV GIDTGKFIKS LRRGEAGAVK SAGWAAAAKA WGPGNSVASV ALTGAYYMPT
SLVQKVTDVA RALVGKDTVP QYRPELSKGG VKRSKAFGTR IGAPGVEPTG VFVPACVNSM
FGPQSDGVGA SEAFAKLVER AGLALTVPEG IDGMCCGTPW TSKGMSTGHD IMQRRVNDQL
IAATDGGRLP VVVDASSCTH GFRDMAESIG ITVIDAIEFV EQHVLANLEV THKVPSVTLH
PTCSATHLGI VETLKHVAAA AAEDVRVPAE WNCCGYAGDR GMLHPELTHA ATKREAAEAK
ELGSACHASS NRTCELGLTA ATGKDYEHIL EILERASR
//
