ID G8NXU5_GRAMM Unreviewed; 969 AA.
AC G8NXU5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:AEU34440.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:AEU34440.1};
GN OrderedLocusNames=AciX8_0082 {ECO:0000313|EMBL:AEU34440.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU34440.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU34440.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP003130; AEU34440.1; -; Genomic_DNA.
DR RefSeq; WP_014263324.1; NC_016631.1.
DR AlphaFoldDB; G8NXU5; -.
DR STRING; 682795.AciX8_0082; -.
DR KEGG; gma:AciX8_0082; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_010756_0_0_0; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000007113; Chromosome.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 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; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AEU34440.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113}.
FT DOMAIN 56..284
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 969 AA; 106501 MW; C0C751F6298EC534 CRC64;
MSTQPLTILR APAAKTPFNP FPAATDLEAH LRRTVRGEVR FDQGTRALYA TDASNYRQIP
IGLVLPLDSA DIEATLAACR EFNAPVLARG AATSLAGQCC NTAVILDFSK YMRRVLAVDP
ESRTARVEPG VVLDRVREAA EEHELTFAPD PATHSRCTLG GMIGNNSCGT HSLLGGKTVD
NIESLDILLY DGTRMTVGPT SEEQLEAIIA GGGRQGEIYA GLKKIRDQYA ALIRQRFPRI
PRRVSGYNLD ELLPEQGFNV ARALVGSEGT CVTILEAKLR LVKSPQFRRL VGIGFSDAFI
AADNVPLVLE HNPIALEGFD GLLVEFMQRK NLATEEVRLL PDGKGYLLAE LGADSAEEVE
AKAQTLVAAA QQFAARPSVR LYTAEEARKV WFVRESALGA TAFVPGEPVG WEGWEDAAVA
PQELGEYLRA ICTLMQEYGY RSPMYGHFGH GCVHLRINFD FKSERGIAIY REFVDRATDL
VVSLGGSISG EHGDGQSRGA LLEKMFGAEL MEAFREFKRL WDPLARMNPG KLIDAYQPHD
YLRLNTSHAP IQTSTHFHFA SDGGSFEQAA LRCVGVGACR KEEAGTMCPS YMATKEEKHS
TRGRAHLLWE MMQGDVVRDG WRSEEVREAL GLCLACKACK TECPVNVDMA TYKAEFLAHH
YEGRLRPLGA YAFGFVDKGA RLASLAPGIA NFMTSWPLTS RLAKAALHIH PDRTLPSFSS
QTFRKRSKAL RQPAQPKGDV LLWADTFNNY LHSDTAVAAH KVLVDAGFRV HVLQQHVCCG
RPLYDFGLLD SAKKYLLKTL DALAPYAEMP VVVLEPSCAT VFRDELMNLR PNDPRASKLR
DRTYLLSQFL VKYAPEYKPP AIGGTILVQG HCHHQAVMKM TDEMQLLRST GADVQLLDSG
CCGMAGPFGF EKDKYEVSQT LAERVLLPAV RGAKAGTLVV ADGFSCREQV AQNSETRALH
LAEVLARGL
//
