ID A9WF31_CHLAA Unreviewed; 887 AA.
AC A9WF31;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ABY35346.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:ABY35346.1};
GN OrderedLocusNames=Caur_2134 {ECO:0000313|EMBL:ABY35346.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY35346.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000909; ABY35346.1; -; Genomic_DNA.
DR RefSeq; YP_001635735.1; NC_010175.1.
DR AlphaFoldDB; A9WF31; -.
DR SMR; A9WF31; -.
DR STRING; 324602.Caur_2134; -.
DR EnsemblBacteria; ABY35346; ABY35346; Caur_2134.
DR KEGG; cau:Caur_2134; -.
DR PATRIC; fig|324602.8.peg.2417; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_015554_0_0_0; -.
DR InParanoid; A9WF31; -.
DR OMA; PLRMRYG; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 2.
DR Gene3D; 3.30.70.2740; -; 1.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 2.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 2.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 2.
DR PROSITE; PS51387; FAD_PCMH; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ABY35346.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002008}.
FT DOMAIN 51..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 499..671
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 887 AA; 93525 MW; 34325EF12D638EC4 CRC64;
MALQAKEQYT VTPVVVPDKL VAELRAILGA DAVVTAPEAL LTYDSDGSMI VSHPPQLVVL
PKDAGQVATA VRLAVREGLA VVARGAGTGI AGGAVPLCGG LLISTARMTD ITTVDVRSRL
AVVQPGVVNA DLNAHLAPLG YQFAPDPSSQ RASTIGGNIA TNAGGPHCLK YGVTSNHVLA
VEVVDHTGQR YWTGDGVIDP VGYDLTGLLV GSEGTLGVVT AAIVRLTPLP EAVRVVLALF
PTVVAAAAAV SAVIASGSLP TSLEVMDHNA IRAVNSAYSL GLPETTGTTA LIIEVDGVQD
GLDDQLDQII AICRDHGAFD LRPARDPATQ ARVWMARKSV AGAIGRLAPA YYLVDTVVPR
TRLPLMMEHV ERLRAEYGME VCNVFHAGDG NLHPLVLYDP RDPDQRQRAH AIAAGVLELS
IEHGGVVSGE HGIGLEKCEY LPRFFSPAEL QLHATIHQVF NPTGCFNPAK IFPSDTPPAD
LAAARAMRLQ QRDPASVTSA PAPGSCVAPA TPDAAAELLR VCHHAGLPVV PTGGCTARSP
TAVTVSTQHW RGALVYEPDD LTIKVAAGTT LAELQSLLAP HRQMIPLDVA DAQRSLGSLV
ATAVDGPRRL GYGSFRDWVL ALDVIEPDGI PVRLGAQVVK NVTGYDLVKL YVGSAGTLGL
ITAVALKVFP QPPASATLLA HLSTPTAAWT LIDHLAASRL LPTAVEYLAD TQAIVVAMRA
EGHPAAVERH MREATALAHR HDVSVTVLRD VEETTFWQQT VARYAPIANG VLLRVGVWPA
QCATAIQTIE QCAARHQVAI EITAHALSGI IYIQTIGDFT AIAAFHADLV AAFPHTRILA
APPMFVPQAS VWGQPPVALS RMQALKVAID PHNHMNPAAF WFSDTRV
//