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 02-NOV-2016, entry version 28. DE RecName: Full=Respiratory nitrate reductase subunit alpha; DE EC=1.7.99.4; 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; Halobacteria; Haloferacales; Haloferacaceae; OC Haloferax. OX NCBI_TaxID=523841; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME RP REGULATION, SUBUNIT, INDUCTION, SUBCELLULAR LOCATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / RC R-4; RX PubMed=15342113; RA Lledo B., Martinez-Espinosa R.M., Marhuenda-Egea F.C., Bonete M.J.; RT "Respiratory nitrate reductase from haloarchaeon Haloferax RT mediterranei: 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 / RC 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., RA Chen Y., 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 / RC R-4; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [4] RP ENZYME REGULATION, SUBCELLULAR LOCATION, SUBUNIT, AND PUTATIVE RP REACTION 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., RA Butler C.S., 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 CC nitrate as a terminal electron acceptor during anaerobic CC conditions. The alpha chain is the actual site of nitrate CC reduction (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced CC acceptor. {ECO:0000269|PubMed:15342113}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC 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) CC (Mo-bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- ENZYME 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 CC of 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. CC {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 CC an alpha and beta chain is proposed to associate with additional CC subunits 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 -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01004}. 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_CP007553.1. DR EnsemblBacteria; AFK20939; AFK20939; HFX_5104. DR EnsemblBacteria; EMA05271; EMA05271; C439_00690. DR GeneID; 13025838; -. DR KEGG; hme:HFX_5104; -. DR KO; K17050; -. DR OMA; WQRPPRH; -. 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:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su. 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; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Membrane; Metal-binding; Molybdenum; KW Nitrate assimilation; Oxidoreductase; Plasmid; Signal; Transport. FT SIGNAL 1 ? Tat-type signal. {ECO:0000255}. FT CHAIN ? 984 Respiratory nitrate reductase subunit FT alpha. FT /FTId=PRO_0000428886. FT DOMAIN 103 167 4Fe-4S Mo/W bis-MGD-type. FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 110 110 Iron-sulfur (4Fe-4S); via pros nitrogen. FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 114 114 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 118 118 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 153 153 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 249 249 Molybdenum. {ECO:0000250}. FT CONFLICT 281 282 SN -> VE (in Ref. 1; CAF21906). FT {ECO:0000305}. FT CONFLICT 429 434 TTVQTQ -> QRSNP (in Ref. 1; CAF21906). FT {ECO:0000305}. FT CONFLICT 564 566 NTD -> TPN (in Ref. 1; CAF21906). FT {ECO:0000305}. FT CONFLICT 603 603 W -> R (in Ref. 1; CAF21906). FT {ECO:0000305}. FT CONFLICT 694 694 Q -> L (in Ref. 1; CAF21906). FT {ECO:0000305}. FT CONFLICT 709 709 K -> R (in Ref. 1; CAF21906). FT {ECO:0000305}. FT CONFLICT 833 833 P -> S (in Ref. 1; CAF21906). FT {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 //