ID   Q2IDT2_ANADE            Unreviewed;       955 AA.
AC   Q2IDT2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   OrderedLocusNames=Adeh_2973 {ECO:0000313|EMBL:ABC82743.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC82743.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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; CP000251; ABC82743.1; -; Genomic_DNA.
DR   RefSeq; WP_011422025.1; NC_007760.1.
DR   AlphaFoldDB; Q2IDT2; -.
DR   STRING; 290397.Adeh_2973; -.
DR   KEGG; ade:Adeh_2973; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   eggNOG; COG1145; Bacteria.
DR   HOGENOM; CLU_013688_0_0_7; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000001935; 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   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   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:UP000001935}.
FT   DOMAIN          41..269
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          532..563
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   955 AA;  100937 MW;  A2A13BBA28436588 CRC64;
     MRALPEPYRR LHEALARHLP GERLVTDPLR RLALGTDASF YRLTPRLVVE VRTVDEVRRV
     LAEAARLGTP VTFRAAGTSL SGQAVTDSVL VRVTGGWRGL RVLDGGARIA LEPGVIGADA
     NAVLAPLGRK LGPDPASIGA CMVGGIAANN ASGMCCGTAQ NSYRTVASMR LVLADGTELD
     TADPASREAF RAARPEVVAG LQAIRAEIEA DPALRRRIVE KFRIKNTTGY ALNAFVDFED
     PVDVLLHLMI GSEGTLGFIA EVTYHTVPEH AHKASALALF AGVGDAARAT MLLQGGPVAA
     VELMDRASLR SVEAKPGMPP ELAGLPEGAA ALLIETRAAT PAGLGPQVDA LLARMAPVPA
     LAPVRFTAVK AETERLWDVR RGLFPAVGAA RPVGTTVVIE DVAFPIRHLA DATVALQGLL
     AAHGYDGIIF GHALDGNLHF VFTPDFGAEG EVERYARFMD DVCTMVARRY DGSLKGEHGT
     GRNVAPFVEL EWGAKATGLM RRVKRLLDPG GLLNPGVVLN DDPQAHLRHL KALPHAHPIL
     DRCIECGFCE PRCPSRDLTL TPRQRIVAQR EIARLRVTGE DPAALDRLER DYVYLGEQTC
     AVDGLCATAC PVGIDTGEHT KWLRAQAHAD GSGAADLAAD RFAAVAAGAR AGLRLASAAH
     AVLGTAALGG LTRGLHRLSA GRLPVWNEAT PRAARAPRLD GTRRGGGRVV YFPSCVSRTM
     GPARGDEEGA EVHAAMLSLL GKAGLDVVFP PGMEGLCCGM PFESKGWPAQ ADRKRRELEA
     ALLEASEGGR HPVVFDTSPC VYRMRKAAGG RVAIHDPVEF IQRFVLPRVT LARVPGPVAV
     HVPCSAVKLG LGPAFRAVAE ACAEQVVLPR EVGCCGFAGD RGFTHPELTA SALAPLAAAL
     PAGCAAGFSS SRTCEIGLSL HAGVPYRPLA WLVDRCASPR AAPDLEPPSP RTHLA
//