NARB_HALMT
ID NARB_HALMT Reviewed; 220 AA.
AC I3R9N2; Q703H9;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Putative respiratory nitrate reductase subunit Rieske;
GN Name=narB; OrderedLocusNames=HFX_5107; ORFNames=C439_00675;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OG Plasmid pHM300.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=15342113; DOI=10.1016/j.bbagen.2004.05.007;
RA Lledo B., Martinez-Espinosa R.M., Marhuenda-Egea F.C., Bonete M.J.;
RT "Respiratory nitrate reductase from haloarchaeon Haloferax mediterranei:
RT biochemical and genetic analysis.";
RL Biochim. Biophys. Acta 1674:50-59(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
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).
RN [4]
RP PUTATIVE REACTION MECHANISM, AND SUBUNIT.
RX PubMed=17888006; DOI=10.1111/j.1574-6968.2007.00887.x;
RA Martinez-Espinosa R.M., Dridge E.J., Bonete M.J., Butt J.N., Butler C.S.,
RA Sargent F., Richardson D.J.;
RT "Look on the positive side! The orientation, identification and
RT bioenergetics of 'Archaeal' membrane-bound nitrate reductases.";
RL FEMS Microbiol. Lett. 276:129-139(2007).
CC -!- FUNCTION: The respiratory membrane-bound nitrate reductase enzyme
CC complex plays a role in generation of metabolic energy by using nitrate
CC as a terminal electron acceptor during anaerobic conditions. Proposed
CC Rieske subunit involved in a protonmotive Q-cycle mechanism-based
CC electron transfer electrons to the beta subunit.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: Probable multiprotein complex; a catalytic heterodimer of an
CC alpha and beta chain is proposed to associate with additional subunits
CC involved in membrane attachment and electron transfer.
CC {ECO:0000269|PubMed:17888006}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein.
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DR EMBL; AJ621877; CAF21903.1; -; Genomic_DNA.
DR EMBL; CP001870; AFK20942.1; -; Genomic_DNA.
DR EMBL; AOLO01000001; EMA05268.1; -; Genomic_DNA.
DR RefSeq; WP_004056326.1; NZ_CP039141.1.
DR AlphaFoldDB; I3R9N2; -.
DR SMR; I3R9N2; -.
DR EnsemblBacteria; AFK20942; AFK20942; HFX_5107.
DR EnsemblBacteria; EMA05268; EMA05268; C439_00675.
DR GeneID; 40158243; -.
DR KEGG; hme:HFX_5107; -.
DR HOGENOM; CLU_096353_1_0_2; -.
DR OMA; CTHAGCM; -.
DR OrthoDB; 67221at2157; -.
DR Proteomes; UP000006469; Plasmid pHM300.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cell membrane; Disulfide bond; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Nitrate assimilation; Plasmid;
KW Transport.
FT CHAIN 1..220
FT /note="Putative respiratory nitrate reductase subunit
FT Rieske"
FT /id="PRO_0000428890"
FT DOMAIN 118..206
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 151
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 153
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 168
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 171
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 156..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 88
FT /note="V -> L (in Ref. 1; CAF21903)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..140
FT /note="TEYM -> RNT (in Ref. 1; CAF21903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 23089 MW; 2705FEFD38B7ABAC CRC64;
METDRQGSES GACDGCCSDC SDEGTQSQQP TIFTDTRASL ARRDYAKLLA SVGGLTAVAS
LTAPLAGLTR VFEREYTGPV YSDGIYLVDG DGNRIEEKAL SEGEKMTVFP EPRPGIEKAP
TLLVRHAEDA YSDAVKTEYM VAGYTAYSKV CTHAGCMVSN EEDGTLVCPC HFGKFDPTDG
AAVVGGPPSR ALPQLPITVS SEGYLIATGD FNGPVGPGGD
