ID   L9XSZ7_9EURY            Unreviewed;      1011 AA.
AC   L9XSZ7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ELY64491.1};
GN   ORFNames=C489_17099 {ECO:0000313|EMBL:ELY64491.1};
OS   Natrinema versiforme JCM 10478.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY64491.1, ECO:0000313|Proteomes:UP000011632};
RN   [1] {ECO:0000313|EMBL:ELY64491.1, ECO:0000313|Proteomes:UP000011632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY64491.1,
RC   ECO:0000313|Proteomes:UP000011632};
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:ELY64491.1}.
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DR   EMBL; AOID01000051; ELY64491.1; -; Genomic_DNA.
DR   RefSeq; WP_006432520.1; NZ_AOID01000051.1.
DR   AlphaFoldDB; L9XSZ7; -.
DR   STRING; 1227496.C489_17099; -.
DR   PATRIC; fig|1227496.3.peg.3447; -.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000011632; 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; -; 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   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; 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          64..300
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          644..677
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  109093 MW;  1B3C761AC6EE5EFE CRC64;
     MAAEDSSVDA TVEDRDHGRR DRPLESGSDG DGEALAADLR DAVDGDVRFD EYTRVLYATD
     GSIYGAQPAG VVFPRDTADV RAAMAVAADH DAPVLPRGSG SSLAGQTVGP GCVVLDLSRH
     MDEIREIHPA ARTAVVQPGV VQDDLDAALE PHGLRFAPDP ASSNRATIGG GIGNNSTGAH
     SVRYGITDAY VDECEVVLAD GSQIRTRDVA LDSPEWDRIV SKDDREAALY RTVRALVEDH
     AAEIEERYPD LKRSVSGYNL QKVIRETADG DRVINLSKLL VGAEGTLGVV VEATLSLVTR
     PDETALAVYC YDDLLEALAA VPEALDLKAS AVELMDDEVF RLAAESAEYA EYAEPIPEGT
     EAALMLEFDS EVVDDLPDAI ATATAGLVDS GTAFGSIEAF SPAKQDRLWK LRKAAIPLLM
     SMDGDPKPYP FVEDASVPPV ELAEYVAGFQ EILEAHDTTA AYFAHAGVGT LHIRPVLNLK
     AADDVEKMRA IADDVTDLVR EHNGSFSGEH GDGLARTEFN PKLYGPELWD AFQDLKSAFD
     PDWRLNPGKV VYREDDPTDI RDHLRYGPDY AALEPRTTLD FDDEGGFADL VELCNGCGTC
     RQTDGDVMCP TYRATEEEIA TTRGRANLLR AAISGEIDPE ELYGERFQDE VLDLCIGCKG
     CQSDCPTGVD LAKLKAEVKH QYHDREGTSL RERLFANVDR LAAVGSAFAP LANRAAELPG
     ARTVLEKTVG IAADRTLPTF RRESLVDWFR QRGGPRVAAE TATAGVVLFP DTDTNYSNPE
     LGKAAVAVLE AANVRVVVPD LGPTGRAAYS TGMLDVAAEQ GRDLLADLEP YLERGWSVLF
     VEPSDAAMVV DEYRSLLADE RVERLAANAF GVCEYVDERR LDEELTFVQS ENADTRLSFH
     GHCHQKARGA DHHAVGVLRR AGYAVDPVDS SCCGMAGSFG YEAEHYDLSK AIGSLLREDL
     EASAAGRADG DGESIVVAPG TSCRTQVGDF EGYDRPAHPV ELLARGLEPS D
//