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
//