NARG_BRASZ
ID NARG_BRASZ Reviewed; 902 AA.
AC P85097;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Respiratory nitrate reductase alpha chain;
DE EC=1.7.5.1;
DE AltName: Full=Respiratory membrane-bound nitrate reductase subunit alpha;
DE Flags: Fragments;
GN Name=narG;
OS Bradyrhizobium sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=376;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=USDA 3045 {ECO:0000269|Ref.1};
RA Polcyn W.;
RT "Identification of membrane-bound respiratory nitrate reductase from
RT Bradyrhizobium sp. (Lupinus) USDA 3045 by tandem mass spectrometry.";
RL Submitted (FEB-2007) to UniProtKB.
CC -!- FUNCTION: The nitrate reductase enzyme complex allows Bradyrhizobium
CC sp. USDA 3045 to use nitrate as an electron acceptor during anaerobic
CC growth. The alpha chain is the actual site of nitrate reduction.
CC {ECO:0000250|UniProtKB:P09152, ECO:0000269|Ref.1}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P09152};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P09152};
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 micromolar concentrations of azide.
CC {ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC Alpha and beta are catalytic chains; gamma chains are involved in
CC binding the enzyme complex to the cytoplasmic membrane.
CC {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.1}. Cytoplasm
CC {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Induced by anaerobiosis, there is no significant expression
CC in an aerobic environment. Expression is further induced in the
CC presence of nitrate or nitrite. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000255}.
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DR AlphaFoldDB; P85097; -.
DR SMR; P85097; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Molybdenum;
KW Nitrate assimilation; Oxidoreductase; Transport.
FT CHAIN 1..>902
FT /note="Respiratory nitrate reductase alpha chain"
FT /id="PRO_0000283778"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P09152"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P09152"
FT NON_CONS 6..7
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 26..27
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 40..41
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 66..67
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 79..80
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 101..102
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 120..121
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 126..127
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 146..147
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 157..158
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 170..171
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 179..180
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 196..197
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 212..213
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 225..226
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 235..236
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 252..253
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 273..274
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 281..282
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 290..291
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 304..305
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 330..331
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 338..339
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 353..354
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 359..360
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 367..368
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 379..380
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 406..407
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 420..421
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 436..437
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 452..453
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 465..466
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 481..482
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 493..494
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 507..508
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 513..514
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 522..523
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 529..530
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 541..542
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 553..554
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 573..574
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 599..600
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 610..611
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 622..623
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 649..650
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 658..659
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 668..669
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 676..677
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 686..687
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 700..701
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 711..712
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 724..725
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 733..734
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 746..747
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 757..758
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 773..774
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 782..783
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 794..795
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 807..808
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 829..830
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 843..844
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 852..853
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 884..885
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 902
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 902 AA; 101519 MW; 93540162AA633C66 CRC64;
FSPIDRYNDN HTQETYEDRE WENVYRSTHG VNCTGSCSWK DGIVTWEGQE LNYPTTGPDM
PDFEPRGASY SWYLYSANRG VLWSMWQEEL QNNESPLDAW KSSWQEVNEL IAASNVYTVK
TYGPDRVAGF SPIPAMSMVS YASGARTPDA HFFTEVRVVS VSPDFAESTK LCDLWLAPKQ
GTDAAMALAM GHVMLREFHL DNPSDYFLNY CRQYTDFPFL VTLSKQKGDQ FVADRAADLV
DALGQENNPE WKPVLWNENT NDFATPHGTM GSRGKWNLEQ RLEDEETGEK LSVLGIEDEI
GTVRLQLADG STALVTTVYD LTMANYGLER GLGGQEPKDF NDDVPFTPAW QEKITGVPRE
LIIQIAREFA DNADKTHGRA VLNLVLLVGA QGVNGGGWAH YVGQEKLRPA EGWQTIAMAK
HMNSTSYFYN HSSQWRYETV TAQELLSPMA DKYQHHGDYN VLAARMGWLP SAPQLGTNPL
RQAGMSPVDY TVKFAAEQPE NGKNHPRNLF VWRSNLLGSS GKGHEYMLKY LLGTENGIQG
KQGGVKPEEV EWKLSSTCLY SDIVLPTATW YEKDDMNTSD MHPFIHPLSA AVDPAWESKS
DWDIFTSLSK KFSEVCVGHL GKETDVVTLP IQHDSAAELA QPLDVKDWKG ECEPIPGKTM
PQIHVVERDY PATYERFTSI GPLMEKGIAW NTQSEMDLLR AWAALSEFTG RDHTHLALNK
EDEKFRDIQA QPRTVITSPA FTGSEKQSFY LDHDMMKDFG ESLLVYRPPI DTRKSRPEVE
GKEITLNYLT PHNKGGPIVW ISETDARDLG IEDNDWIEVF NSNGALTARV PAGMTMMYHA
QERGGIHNSV TRPTHMIGGY AQLAYGFNYY GTVGSNRDEF VVVRNINWLD GEGNDQVQES
VK
