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Database: UniProt
Entry: L9W0Z1_9EURY
LinkDB: L9W0Z1_9EURY
Original site: L9W0Z1_9EURY 
ID   L9W0Z1_9EURY            Unreviewed;      1026 AA.
AC   L9W0Z1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ELY43125.1};
GN   ORFNames=C494_19037 {ECO:0000313|EMBL:ELY43125.1};
OS   Natronorubrum bangense JCM 10635.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronorubrum.
OX   NCBI_TaxID=1227500 {ECO:0000313|EMBL:ELY43125.1, ECO:0000313|Proteomes:UP000011690};
RN   [1] {ECO:0000313|EMBL:ELY43125.1, ECO:0000313|Proteomes:UP000011690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10635 {ECO:0000313|EMBL:ELY43125.1,
RC   ECO:0000313|Proteomes:UP000011690};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELY43125.1}.
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DR   EMBL; AOHY01000058; ELY43125.1; -; Genomic_DNA.
DR   RefSeq; WP_006067921.1; NZ_AOHY01000058.1.
DR   AlphaFoldDB; L9W0Z1; -.
DR   STRING; 1227500.C494_19037; -.
DR   GeneID; 39852780; -.
DR   PATRIC; fig|1227500.6.peg.3844; -.
DR   eggNOG; arCOG00337; Archaea.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000011690; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
FT   DOMAIN          60..303
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          670..703
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  111907 MW;  DB07F60B70146227 CRC64;
     MTITPPNRLD PADDPEANYN YQSDDIERPD LLADLEARVD GDVRFDSYSR QLYATDASIY
     EVTPIGVVFP TSTDDVASVV SYCADNEIPV LPRGGGTSLA GQTVNEAVVL DFTTYMDDVV
     DIDPDARRAT AQTGIYLGSF NEALAPHELK FAPDPAWGDK SALGGAIGNN TTGAHSLQYG
     KTDAYVEEVE VVLADGTVTT FGEVDLEDVP ELADGDDLES AIYAEVARIL EEQGDLIDDV
     YPDLKRNVSG YNLDWLVEDA YGGERGIGEP DSEGGTINLA KLLCGSEGTL AIVTEATVSL
     ETIPEEKSMA LLAYDSVLEA MDDVEPIVEH DPAAVEVLDD VMIDLARDTP EFAPVTEMLP
     DGTAAVLIVE FYADDVDDGK RKVANLLADR CPSVESEGEA DDEDERTITG ADTLAFDAIE
     AYDADSRAKI WKLRKSGLPI LLSRTTDEKH VAFIEDTGIP PANLRAFVAD FQEVLEDHDT
     YASFYAHAGP GVLHIRPLVN TKTDAGLEDM ESITDAVTDL VVKYDGSVSG EHGDGRARTQ
     WNRKLYGEAV WETFQELKTA FDPDWLLNPG QVVYRDDDPT DMTKNHRFGP DYEFNAGFEP
     ALEWDNDQGF QGMTELCHGC GGCRGEQSTT GGVMCPTFRA EDEEILSTRG RANMLRQAMS
     GELEPDEQFD DEFVEEVLDL CIGCKGCKHD CPSGVDMAKL KAELTYEHHK RNGVSLRDQF
     FTNFETLAKL GSATAPVSNW MAKLPGSGVL TEKLLGISRE RDLPTFQRNT FAKRVADHRP
     AVPAREADRR VVLVPDIYTN HEYPEAGEAA LAVLEAAGVH VEIADPRDVG RPAYSKGLLG
     QAAEDATDTV HELLPYVEDG YDVVLIEPSD AVMVQSDYLD LFDHPEVEAV ATNTYGVCEY
     IDQFDLDADI EFAAPDEHLA YHGHCHQKAH AKDHHAVGVL RRAGYAVDPL DSTCCGMAGS
     FGYEVEHYSM SKAIGEVLYE QVDDSTAERV VAPGASCRTQ LEDRPGATEK PPTPIEVVAA
     ALAGRR
//
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