ID F8DCA3_HALXS Unreviewed; 1124 AA.
AC F8DCA3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:AEH38360.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:AEH38360.1};
GN OrderedLocusNames=Halxa_3754 {ECO:0000313|EMBL:AEH38360.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH38360.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH38360.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP002839; AEH38360.1; -; Genomic_DNA.
DR RefSeq; WP_013881247.1; NC_015666.1.
DR AlphaFoldDB; F8DCA3; -.
DR STRING; 797210.Halxa_3754; -.
DR GeneID; 10798697; -.
DR KEGG; hxa:Halxa_3754; -.
DR eggNOG; arCOG01491; Archaea.
DR eggNOG; arCOG01492; Archaea.
DR HOGENOM; CLU_000422_1_1_2; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000006794; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEH38360.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006794};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 54..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 452..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 124479 MW; CD3B9806564F833D CRC64;
MSAGEDPVTI DLDRRSFVKA SALAGGVFLG GGAAGHALGG TQEEQGDDGV PEGEETSKVI
CNYCAVGCGF KAVKDGNSFV GQEPWFENPI NNGSLCSKGA GILETEHSPK RLKHPMRKED
GEWRRVTWDD AFREIADTWE QTIEEYSRES VMFLGSAHHS NEAAYASRKF AAFMGTNNVD
HQARICHSPT VTGLANTWGF GAMTNTINDY RNFDLLIILG QNPAESHPIA MQHILEGQAR
GGTIVSIDPR YTKTSAHADY FYRLRPGTDV ALVMGLLNYI NEQDELDDEF LAGRVMGWPD
VESELEQYDL ETVSDITWID QGDLEEIGDL IIENKPQIQV EWAMGGTQHN NGTQNIRSYA
IFSLATGSAA RSGGGLQVMR GHANVQGATD LGVDASILPG YYGVDAPGSW EHWADVWDRS
PWTSGSTSFE ELYEKFELLP EDVWEGTQTP AEVEAGGAGV DVEEEAAGEG GEGEADVQGE
DEEAEGDEDA GDEEEEEEGL QAEAPIDDVE ERSMMFQIGL TVARWYEAAL EQGDRLLESN
LYQPDPLKMA FFWGHSANSI SEMDKMKQAM ENLDLLVVVD VFPAVAGTLP DDADVLLLPA
SSQYEHVRTV TNSHRSVQWS EAVAEPAHNS KPDLQIMQEL AQYMGFGEHF DWGNGPEVHN
GRSSYEDALR EINLGVRSIG YQQPPEKLQQ HHEYDWAFNA DDLRAQNTGT PVDGDYWSLP
WPYWGDDHPG SPIIWTKEAD PRDGGHDFRE NWGVRAPTAE EWNDLEIDKE YPLQETYDEH
GEDGLDLIAE SFEAPWWDDQ EIEGVPSYPG YSTVLPDDPT NPSTQTTPVE MALDEEQSVY
DAAQAVAEQY DDIGVDPSAY EEYDNAQPDP PTGRGKARAV VWNFLDTVPV HREPVESPRP
DLVEEWPANG EQRNFWRLDQ NNATVQQRAT EAVHTELGSD SQNGRTVILT SGRQVEHQGG
GAETRNNEYT ADRQPHMYAE ISPALAEALD VVGGDDHVIV ESADKGAILV KAKVTNRVND
EEIFLPYHWG GVFHGEDLTP NWPDGTEPLA IGESANIITP SGFDAETQMQ ETKSGVVHVQ
KATQSVVDDY DMEFIDYPQD EHGLGAQKQY DVREWDMYEG GEQL
//
