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Database: UniProt
Entry: W0JNG4_9EURY
LinkDB: W0JNG4_9EURY
Original site: W0JNG4_9EURY 
ID   W0JNG4_9EURY            Unreviewed;      1065 AA.
AC   W0JNG4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=HALLA_06425 {ECO:0000313|EMBL:AHF98532.1};
OS   Halostagnicola larsenii XH-48.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF98532.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHF98532.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHF98532.1,
RC   ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JAN-2014) 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; CP007055; AHF98532.1; -; Genomic_DNA.
DR   RefSeq; WP_049951744.1; NZ_CP007055.1.
DR   AlphaFoldDB; W0JNG4; -.
DR   STRING; 797299.HALLA_06425; -.
DR   GeneID; 25144128; -.
DR   KEGG; hlr:HALLA_06425; -.
DR   PATRIC; fig|797299.3.peg.324; -.
DR   eggNOG; arCOG00337; Archaea.
DR   HOGENOM; CLU_010756_0_0_2; -.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000019024; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 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; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
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; 2.
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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019024};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          58..302
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          692..723
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          391..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1030..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1065 AA;  115081 MW;  5E39002F2D44DAAE CRC64;
     MATEPSDDPA ADARAGYDYA STDVDRPGLV RDLENLVDCS VRFDSYSRQL YATDASPYEV
     TPVGVVFPES TADVARVVEY CARRGVPVLP RGGGTSLAGQ TVNRAVVLDF TRHMNEIVET
     DPDERTATVQ PGTILGTLNE TLEPHDLKFA PDPAWGDKSA IGGAIGNNST GAHSLQYGKT
     DAYVESCEVV LADGTVTRFG EVTLEEIDER GDPDGPLEAR IYAEIARILE EDADAISEAY
     PDLKRNVSGY NLDRLVAEAR GENLPGGEDT GEPGTVNLAR VLAGSEGTLA IVTEATVSLE
     PVPETKSVAL LCYAELRDAM TDVAPIIEHD PAAVEVLDDV LIDLARGTAE FAPVTEMLPE
     GTNATLLVEF YAEDDSEGRE RVAELLADRC PSVTPAGASD GGVSKVDSSA DDTSGNGSSG
     ADSNTTASGD AQPVAIDALE AYEDAERAKL WKLRKSGLPI LLSRTTDEKH ISFIEDTAIP
     PERLPEFVDR FESILESHDT YATFYAHAGP GVLHVRPLVN TKTDTGIDQL RGIADDVTDL
     VVELGGSVSG EHGDGRARTQ WNRKLYGEDL WVTFRDLKSA FDPDWLLNPG QVVFRDENPT
     DLRENLRFDP DYEYDAGFEP TLEWNNDNGM QGMVELCHGC GGCRGEQSTT GGVMCPTYRA
     SHEEITSTRG RANSLRQAMS GDLPRGEQFS DEFTEEVMDL CIGCKGCAID CPSEVDMAKL
     KAEVTHEYHQ RNGASLRDRL FANVANLSRW GSRFAPLSNV AHRIPGSRWL LEKTVGIASD
     RPLPTFHSDT FSDWFERRGG TAVEEVDAER EVVLYPDTYT NYNHPEAGKA AVRVLEAADV
     HVTVPNGVGD TGRPAFSKGF LDKARETARD NVESLSPHLE EGRDIVLIEP SDAVMLQSDY
     LDLLGEDARA LAERTYGVCE YLDTFRLDES ISFLSPSDLE PGGDEAAADG ATADGGALEH
     LTYHGHCHQK ATAKDHHAVG VLRRAGYAVD PLDSGCCGMA GSFGYEAEHA SMSNAIADVL
     YEQVDSSEGE RVVAPGASCR SQLEGRPDAE EEPPTPIEML ANALE
//
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