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Database: UniProt
Entry: A0A0G3CG04_9GAMM
LinkDB: A0A0G3CG04_9GAMM
Original site: A0A0G3CG04_9GAMM 
ID   A0A0G3CG04_9GAMM        Unreviewed;       938 AA.
AC   A0A0G3CG04;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=QQ39_01460 {ECO:0000313|EMBL:AKJ40911.1};
OS   Pragia fontium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Pragia.
OX   NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ40911.1, ECO:0000313|Proteomes:UP000068021};
RN   [1] {ECO:0000313|EMBL:AKJ40911.1, ECO:0000313|Proteomes:UP000068021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24613 {ECO:0000313|EMBL:AKJ40911.1,
RC   ECO:0000313|Proteomes:UP000068021};
RX   PubMed=26159528;
RA   Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT   "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT   Bacterium from the Family Enterobacteriaceae.";
RL   Genome Announc. 3:e00740-15(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP010423; AKJ40911.1; -; Genomic_DNA.
DR   RefSeq; WP_047779662.1; NZ_CP010423.1.
DR   AlphaFoldDB; A0A0G3CG04; -.
DR   STRING; 82985.QQ39_01460; -.
DR   KEGG; pfq:QQ39_01460; -.
DR   PATRIC; fig|82985.3.peg.310; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000068021; 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   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   4: Predicted;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068021}.
FT   DOMAIN          38..266
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;  103417 MW;  75097CD617CAC517 CRC64;
     MKASYQTFYR ELCRFVPKEC IYTDPSRTMA YGTDASCYRL IPQIVVRLDS EKQVQQTLVL
     AQKHGHPVTF RAAGTSLSGQ AITDSILITL GDNWRQYKIF ADAGYISLKP GVIGADANRY
     LAPFGRKIGP DPASIDACKI GGIAANNASG MCCGTAQNSY QTLQAMRLIL ADGTLIDTAD
     SESVSAFKKT HNAMLEQLQT LSQQTKNNHH LAELIRHKYR LKNTTGYSLN ALVDFDDPLD
     ILTHLMIGSE GTLGFIAEIT YQTVEEHQFK ASALFVFSDI EAACEATRIL KQQPVSAVEL
     MDRGALASVE NEAGLPDFMP NLSEDATALL VEVRSADAEG LKEKMAQIMS SISTFTLEQQ
     VPFTDKPEEF GRLWAIRKGI FPAIGAVRPV GSTVIIEDVA FPIEQLAAGV RDLRKLFIKH
     DYNAVIYGHA LDGNMHFVFQ QSFDSPEQVR RYQVFMEDIA QLVAVEYKGS LKAEHGTGRN
     MASFVELEWG SEAYELMWQL KNLLDPHHLL SPGVLLNRDH QAHLQNLKLL PAADKRVDSC
     IECGFCEPVC PSTNLSFTPR QRIVIWREIN RLRRSGDDNQ RLKQLEKDFR YLGDDTCAAT
     GLCARRCPVG INTGELIRDI RTQRNMRYER VARWTADHFT TLTTGARLAL NTVAGAGKVV
     GRERLGKITK ALHVTSAGHI PLLTPSFPKG AHSPTAPKLV AGDLKVVYLP SCASRTMGAS
     ANDADQRPLT EIVEKLLNKA GFSIIYPEKL DSLCCGMPYN SKGITTVAQN KLGDMEQALW
     EASEQGKYPI LIDTSPCALR AVEGFTKPMA LFEPVGFVNH YLADKLHFTP EDKPIMMHVT
     CSSVKMGLSA AMKNLLDRCC TQVIIPDGIH CCGFAGDKGI KTPELNSNAL RLLSQQVPAN
     CSEGVSNSRT CEIGLTEHSG VPYRSILYVV DRVTTPLS
//
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