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Database: UniProt
Entry: A0A285VIY3_9MICO
LinkDB: A0A285VIY3_9MICO
Original site: A0A285VIY3_9MICO 
ID   A0A285VIY3_9MICO        Unreviewed;       951 AA.
AC   A0A285VIY3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=SAMN05421879_102185 {ECO:0000313|EMBL:SOC53827.1};
OS   Ornithinimicrobium cerasi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Ornithinimicrobium.
OX   NCBI_TaxID=2248773 {ECO:0000313|EMBL:SOC53827.1, ECO:0000313|Proteomes:UP000219688};
RN   [1] {ECO:0000313|Proteomes:UP000219688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA17B2 {ECO:0000313|Proteomes:UP000219688};
RA   Varghese N., Submissions S.;
RL   Submitted (AUG-2017) 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; OBQK01000002; SOC53827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285VIY3; -.
DR   STRING; 1122622.GCA_000421185_03282; -.
DR   Proteomes; UP000219688; 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: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   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; 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; 1.
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:UP000219688}.
FT   DOMAIN          51..279
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          543..574
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   951 AA;  100383 MW;  BD74C3C6436C12A7 CRC64;
     MDRASIDHDL GPGPAGGWAR LEEELAASLG EGRVSSRALD RYALAHDASH YLLVPELVVR
     PGDRDQVATV MAACDRAGTS LTFRAGGTSL SGQAVTDTVL VDVRRHFRDV EVLDDGARVR
     VGPGVTVGRV NALLARHGRR LGPDPASESA CTVGGVVANN SSGMQCGTEA NTYATLESLV
     VVLPTGVVLD TGDPGADGQL RAAAPDVHEG LLRLRDRVRG DAGSVATIRR LFALKNTMGY
     GVNAFLDFDE PAQILARLMV GSEGTLGFVA SATFRTVPVR PHVATGLLVF DDVVRATGSV
     PELVAAGTAT AELLDAASLR VSAQDPLCPR LIADLEVVDH AALLVEWQDD ERARLEETVA
     RVQGELGHLP LTVPVSLTRD PVERAGLWRV RKGLYSAVAG ARPAGTNALL EDVVVTVDRL
     GDTILALTEM FERHAYPESV IFGHARDGNV HFMLNEQFAD PASMARYEAF TEDMVDLVLG
     EGGSLKAEHG TGRIMASFVR RQYGDELYEV MCELKRLLDP RGVLNPGSVL SDDPTSYLAD
     LKTAPTVEEE VDRCVECGFC EPVCPSRDVT TTPRQRIVVR REMRAAQLRG DDALAAELAE
     QYEYDGTDTC AVDGMCLTVC PVLINTGDLT RRLRAEASGP VGEVAWRGAA RVWGAGTVAA
     SAALTAARVL PQVPSLMTRA GRTVVDHDAL PRYDRGLPRG GPRRGGTDAA LPGAAAVHFA
     PCVGTMFGPE PATGGVGAER ALVALAGRAG VDLRVPDGVG GLCCGTPWKS KGRRVGYAAM
     AARVLPALLE ASEAGALPVV CEAASCAEGL VQMLGSDPAY REIRVVDATA WVADTLLDRL
     PVTAATGPVV VHPTCSSTHL GTTDALVRVA RHVSDDVTVP VAWGCCGFAG DRGMLHPELT
     AAATAPEAAE VAGREYAAYV SNNRTCELGL TRATGRPYQH VLELLEVATR P
//
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