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Database: UniProt
Entry: D2RVP3_HALTV
LinkDB: D2RVP3_HALTV
Original site: D2RVP3_HALTV 
ID   D2RVP3_HALTV            Unreviewed;      1024 AA.
AC   D2RVP3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ADB59407.1};
GN   OrderedLocusNames=Htur_0509 {ECO:0000313|EMBL:ADB59407.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB59407.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB59407.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001860; ADB59407.1; -; Genomic_DNA.
DR   RefSeq; WP_012941728.1; NC_013743.1.
DR   AlphaFoldDB; D2RVP3; -.
DR   STRING; 543526.Htur_0509; -.
DR   GeneID; 8741090; -.
DR   KEGG; htu:Htur_0509; -.
DR   eggNOG; arCOG00337; Archaea.
DR   HOGENOM; CLU_010756_0_0_2; -.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000001903; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 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; 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;
FT   DOMAIN          58..302
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1024 AA;  111045 MW;  C6F182E0D70C32F8 CRC64;
     MSLESSADPA ADGRANYDYR SDEVDRPALV DDLERLVGCD VRGDSYSREL YATDASPYEV
     TPIAVAFPES TADVVGIVEY CAEREIPVLP RGGGTSLAGQ TVNRAVVLDF TRHMNDILEI
     DPDGRTATVQ PGTILGTLNE ALAPHDLKFA PDPAWGDKSA IGGAIGNNST GSHSLKYGKT
     DAYIEECEAV LADGTVTTFG EVTLEEVADR VDPEGGLEER IYAEVERIIE DEADLIEETY
     PDLKRNVSGY NLDRLVAEAR GSTLPGGEET GEPGTVNLAR LLAGSEGTLA IVTEATVSLE
     SVPETKAVTL LCYPDLHEAM RDVEPILAHD PAAIEVLDDV LIDLARDTAE FGPVTEMLPE
     GTNAVLLVEF YAEDADHGEE LVAGLLADRL PSATPAGKPA SDAPRSDAET LALEALEAYE
     KEERAQLWKL RKSGLPILLS RTTDEKHISF IEDTAIPPAE LPEFVERFEA ILEEHDTYAS
     FYAHAGPGVL HVRPLVNTKT ELGLEQLHGI ADDVTDLVVE LGGSVSGEHG DGRARTQWNH
     KLYGDELWQT FQDLKTAFDP NWLLNPGQVV FREDNPTDLR EHLRFDPDYE FEAGFEPALE
     WDTDNGMQGM VELCHGCGGC RGEQETTGGV MCPTYRASRE EITATRGRAN ALRQAMSGNL
     EPDEAVSDEF VEEVMGLCIG CKGCAIDCPS EVDMAKLKAE VTHEYHQRNG ATLRDRLFAN
     VATLSKWGSQ LAPLSNALPK LPGARSVLES TVGIASDRPL PTFRATTFRN WFDQRGGARV
     SEQAADRSVV LYPDTYTNYS HPDAGKAAVR VLEAANVHVT VPDELGDTGR PAFSKGFLEK
     ARETARENVS KLAPLVEEGR DVVVIEPSDA VMFQLDYLDL LSDERAERVA AATYGVCEYV
     DSFRLDEEIA FDENAAAESL TYHGHCHQKA VAKDHHAVGV LRRAGYAVDP LDSGCCGMAG
     SFGYEAEHAS MSDGIGEILY EQVDASEGDR VVAPGASCRT QLEHRPGTDE SPPTPIELVA
     NALE
//
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