ID NARG_HALMT Reviewed; 984 AA. AC I3R9M9; Q703H6; DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2012, sequence version 1. DT 26-FEB-2020, entry version 47. DE RecName: Full=Respiratory nitrate reductase subunit alpha; DE EC=1.7.5.1 {ECO:0000269|PubMed:15342113}; DE AltName: Full=Nitrate reductase alpha chain; DE Flags: Precursor; GN Name=narG; OrderedLocusNames=HFX_5104; ORFNames=C439_00690; 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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, SUBUNIT, INDUCTION, SUBCELLULAR LOCATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. 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 ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT, AND PUTATIVE REACTION RP MECHANISM. 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. The alpha CC chain is the actual site of nitrate reduction. CC {ECO:0000269|PubMed:15342113}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite; CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; CC Evidence={ECO:0000269|PubMed:15342113}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo- CC bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Inhibited by cyanide, azide and antimycin A. CC Enzyme stability is not dependent on salt concentration. CC {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.82 mM for nitrate {ECO:0000269|PubMed:15342113}; CC KM=0.25 mM for methyl viologen {ECO:0000269|PubMed:15342113}; CC Note=Characterized with purified enzyme corresponding to a dimer of CC NarG and NarH.; CC pH dependence: CC Optimum pH is 8.2. At 40 degrees Celsius (temperature of natural CC environment) the optimum pH is 7.9. {ECO:0000269|PubMed:15342113}; CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. CC {ECO:0000269|PubMed:15342113}; 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:15342113, ECO:0000269|PubMed:17888006}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15342113, CC ECO:0000305|PubMed:17888006}; Peripheral membrane protein CC {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006}; CC Extracellular side {ECO:0000269|PubMed:15342113, CC ECO:0000269|PubMed:17888006}. CC -!- INDUCTION: By nitrate. {ECO:0000269|PubMed:15342113}. CC -!- PTM: Exported by the Tat system. {ECO:0000269|PubMed:17888006}. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ621880; CAF21906.1; -; Genomic_DNA. DR EMBL; CP001870; AFK20939.1; -; Genomic_DNA. DR EMBL; AOLO01000001; EMA05271.1; -; Genomic_DNA. DR RefSeq; WP_004056332.1; NZ_CP039141.1. DR SMR; I3R9M9; -. DR EnsemblBacteria; AFK20939; AFK20939; HFX_5104. DR EnsemblBacteria; EMA05271; EMA05271; C439_00690. DR GeneID; 40158240; -. DR KEGG; hme:HFX_5104; -. DR HOGENOM; CLU_000422_13_3_2; -. DR KO; K00370; -. DR OMA; PFIHPFN; -. DR OrthoDB; 1029at2157; -. DR BioCyc; HMED523841:G1HBL-3243-MONOMER; -. DR Proteomes; UP000006469; Plasmid pHM300. DR Proteomes; UP000011603; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1. DR InterPro; IPR009010; Asp_de-COase-like_dom_sf. DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su. DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR03479; DMSO_red_II_alp; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Plasmid; KW Signal; Transport. FT SIGNAL 1..? FT /note="Tat-type signal" FT /evidence="ECO:0000255" FT CHAIN ?..984 FT /note="Respiratory nitrate reductase subunit alpha" FT /id="PRO_0000428886" FT DOMAIN 103..167 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT METAL 110 FT /note="Iron-sulfur (4Fe-4S); via pros nitrogen" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT METAL 114 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT METAL 118 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT METAL 153 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT METAL 249 FT /note="Molybdenum" FT /evidence="ECO:0000250" FT CONFLICT 281..282 FT /note="SN -> VE (in Ref. 1; CAF21906)" FT /evidence="ECO:0000305" FT CONFLICT 429..434 FT /note="TTVQTQ -> QRSNP (in Ref. 1; CAF21906)" FT /evidence="ECO:0000305" FT CONFLICT 564..566 FT /note="NTD -> TPN (in Ref. 1; CAF21906)" FT /evidence="ECO:0000305" FT CONFLICT 603 FT /note="W -> R (in Ref. 1; CAF21906)" FT /evidence="ECO:0000305" FT CONFLICT 694 FT /note="Q -> L (in Ref. 1; CAF21906)" FT /evidence="ECO:0000305" FT CONFLICT 709 FT /note="K -> R (in Ref. 1; CAF21906)" FT /evidence="ECO:0000305" FT CONFLICT 833 FT /note="P -> S (in Ref. 1; CAF21906)" FT /evidence="ECO:0000305" SQ SEQUENCE 984 AA; 111326 MW; 4CECDC63C15F628E CRC64; MSRNDASQLD DGETTAESPP DDQANDAPEV GDPPGDPVDA DSGVSRRTFL EGIGVASLLG IGTSAASDDS LFQMGGLKPV DDPIGNYPYR DWEDLYREKW DWDSVSRSTH SVNCTGSCSW NVYVKNGQVW REEQSGDYPR FDESLPDPNP RGCQKGACYT DYVNADQRIK HPLKRVGERG EGKWKRISWD EALTEIAEHV VDEVEAGRYD AISGFTPIPA MSPVSFASGS RLVNLLGGVS HSFYDWYSDL PPGQPITWGT QTDNAESADW YNADYIIAWG SNINVTRIPD AKYFLESGYN GTKRVGVFTD YSQTAIHTDE WLSPDSGTDT ALALGMAQTI VDEGLYDEAH LKEQTDMPLL VRQDTGKFLR ASDVPSVNTD ADRPEWMLLM LDSNGRIREA PGSLGERDGQ KDYSKSIELD FDPQLDGETT VQTQSGRVQV RTVWAELRDE LANWDPEMVH EETTVGKETY QRIAREFAEA DKAKIIQGKG VNDWYHNDLG NRALQLLVTL TGNLGEQGTG LDHYVGQEKI WTFHGWKTLS FPTGKVRGVP TTLWTYYHAG ILDNTDPDTA AKIRESIDKG WMPVYPEERD NGSRPDPTTM FVWRGNYFNQ AKGNVAVEEQ LWPKLDLVVD INFRMDSTAM YSDIVLPTAS HYEKHDLSMT DMHTYVHPFT PAVEPLGESK TDWQIFRELA QKIQEVATER GVEPISDRKF DREIDLQSVY DDYVRDWETG EEGALAEDRA ACEYILEHSE ESNPADSDEQ ITFADTVEQP QRLLEAGDHW TSDIEDGEAY APWKDFVQDK NPWPTVTGRQ QYYIDHDWFL ELGEELPTHK EGPENTGGDY PMEYNTPHGR WAIHSTWRDS EKLLRLQRGE PLLYLHPEDA EERGIEDGDS VEVFNDLAEV ELQAKIYPSS QRGTARMYFA WERFQFDSDS NFNSLVPMYM KPTQLVQYPE DSGEHLHFFP NYWGPTGVNS DVRVDVRKAG GGDE //