ID C1DFN6_AZOVD Unreviewed; 938 AA.
AC C1DFN6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN OrderedLocusNames=Avin_43110 {ECO:0000313|EMBL:ACO80432.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO80432.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO80432.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO80432.1; -; Genomic_DNA.
DR RefSeq; WP_012702800.1; NC_012560.1.
DR AlphaFoldDB; C1DFN6; -.
DR STRING; 322710.Avin_43110; -.
DR EnsemblBacteria; ACO80432; ACO80432; Avin_43110.
DR KEGG; avn:Avin_43110; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR eggNOG; COG0479; Bacteria.
DR HOGENOM; CLU_013688_0_0_6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000002424; 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; 3.30.70.2190; -; 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; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
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}.
FT DOMAIN 37..265
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 529..560
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 938 AA; 102740 MW; E9DD072A6B7D7E73 CRC64;
MNLPASFISA VERLIPRERR FDDPLSTLAF GTDASFYRLI PKLVVRVESE AEVVKLLRLA
SASRVPVTFR AAGTSLSGQA VTDSVLIVLG EHWNGRDIRN GGAQIRLQPG VIGAHANAVL
APLGRKIGPD PASINAAKIG GIVANNSSGM CCGTAQNSYH TLAALRLVLA DGSVLDTEDP
LSVARFQASH GELLERLAEL GRQTRADEAL AAKIRHKYRL KNTTGLSLNA LVDYDQPLDI
LTHLMVGSEG TLGFISAVTY HTVPEHPHKA SALIVFPDVE TCCNAVPVLK QQPVSAVELL
DRRSLRSVEN MKGMPDWVKS LSATACALLI ETRASGPSLL AEQIERIMAS IADFPVEKQV
DFSSDPAVYN QLWKIRKDTF PAVGAVRRTG TTVIIEDVTF PIERLAEGVN RLIQLLEKHR
YDEAILFGHA LEGNLHFVFT QGFDEPAQIA RYEAFMQEVA QLVAVEFGGS LKAEHGTGRN
MAPFVELEWG HDAYQLMWKI KRLLDPKGIL NPDVVLSEDP ELHLKNLKPL PAADEIVDKC
IECGFCEPVC PSRGLTLTPR QRIVMWRDIQ ARRRDNAGST ALEKAYRYQG IDTCAATGLC
AQRCPVGINT GDLVRKLRGL DAGHAGTADW LAEHFAASVR ASRLVLLAAD SARRLLGAPR
LEKLSGVLSR ISGGHLPQWT PAMPQPVRLK RPAAAQPDER PRVVYLAACV SRAMGPAGDD
REQVPLLDKT RALLEKAGYQ VVFPKGLDKL CCGQPFASKG YPEQAERKRR ETLDALLEAS
RGGLDPIYCD TSPCTLRLVR EQIDPRLQVF DPVKFIRTFL LERLDFEPQE TPIAVHVTCS
TQHLGEAEAL IDIARRCARE VVVPEGIHCC GFAGDKGFTS PELNANALRT LKEAVQYCEE
GISTSRTCEI GLSRHSGLDY HGLVYLVDRV SRAKARPV
//
