P85097 (NARG_BRASZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Respiratory nitrate reductase alpha chain
EC=1.7.99.4

Alternative name(s):
Respiratory membrane-bound nitrate reductase subunit alpha

Gene names

Name:

narG

Organism

Bradyrhizobium sp.

Taxonomic identifier

376 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length	902 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The nitrate reductase enzyme complex allows Bradyrhizobium sp. USDA 3045 to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction. Ref.1 UniProtKB P09152
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor. Ref.1
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity. UniProtKB P09152 Binds 1 molybdenum ion per subunit By similarity. UniProtKB P09152 Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity. UniProtKB P09152
Enzyme regulation	Inhibited by micromolar concentrations of azide. Ref.1
Subunit structure	Heterotrimer composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane. Ref.1
Subcellular location	Cell membrane. Cytoplasm Ref.1.
Induction	Induced by anaerobiosis, there is no significant expression in an aerobic environment. Expression is further induced in the presence of nitrate or nitrite. Ref.1
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro nitrate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›902	›902	Respiratory nitrate reductase alpha chain		PRO_0000283778
Sites
	Metal binding	29	1	Iron-sulfur (4Fe-4S); via pros nitrogen By similarity UniProtKB P09152
	Metal binding	33	1	Iron-sulfur (4Fe-4S) By similarity UniProtKB P09152
	Metal binding	37	1	Iron-sulfur (4Fe-4S) By similarity UniProtKB P09152
Experimental info
	Non-adjacent residues	6 – 7	2
	Non-adjacent residues	26 – 27	2
	Non-adjacent residues	40 – 41	2
	Non-adjacent residues	66 – 67	2
	Non-adjacent residues	79 – 80	2
	Non-adjacent residues	101 – 102	2
	Non-adjacent residues	120 – 121	2
	Non-adjacent residues	126 – 127	2
	Non-adjacent residues	146 – 147	2
	Non-adjacent residues	157 – 158	2
	Non-adjacent residues	170 – 171	2
	Non-adjacent residues	179 – 180	2
	Non-adjacent residues	196 – 197	2
	Non-adjacent residues	212 – 213	2
	Non-adjacent residues	225 – 226	2
	Non-adjacent residues	235 – 236	2
	Non-adjacent residues	252 – 253	2
	Non-adjacent residues	273 – 274	2
	Non-adjacent residues	281 – 282	2
	Non-adjacent residues	290 – 291	2
	Non-adjacent residues	304 – 305	2
	Non-adjacent residues	330 – 331	2
	Non-adjacent residues	338 – 339	2
	Non-adjacent residues	353 – 354	2
	Non-adjacent residues	359 – 360	2
	Non-adjacent residues	367 – 368	2
	Non-adjacent residues	379 – 380	2
	Non-adjacent residues	406 – 407	2
	Non-adjacent residues	420 – 421	2
	Non-adjacent residues	436 – 437	2
	Non-adjacent residues	452 – 453	2
	Non-adjacent residues	465 – 466	2
	Non-adjacent residues	481 – 482	2
	Non-adjacent residues	493 – 494	2
	Non-adjacent residues	507 – 508	2
	Non-adjacent residues	513 – 514	2
	Non-adjacent residues	522 – 523	2
	Non-adjacent residues	529 – 530	2
	Non-adjacent residues	541 – 542	2
	Non-adjacent residues	553 – 554	2
	Non-adjacent residues	573 – 574	2
	Non-adjacent residues	599 – 600	2
	Non-adjacent residues	610 – 611	2
	Non-adjacent residues	622 – 623	2
	Non-adjacent residues	649 – 650	2
	Non-adjacent residues	658 – 659	2
	Non-adjacent residues	668 – 669	2
	Non-adjacent residues	676 – 677	2
	Non-adjacent residues	686 – 687	2
	Non-adjacent residues	700 – 701	2
	Non-adjacent residues	711 – 712	2
	Non-adjacent residues	724 – 725	2
	Non-adjacent residues	733 – 734	2
	Non-adjacent residues	746 – 747	2
	Non-adjacent residues	757 – 758	2
	Non-adjacent residues	773 – 774	2
	Non-adjacent residues	782 – 783	2
	Non-adjacent residues	794 – 795	2
	Non-adjacent residues	807 – 808	2
	Non-adjacent residues	829 – 830	2
	Non-adjacent residues	843 – 844	2
	Non-adjacent residues	852 – 853	2
	Non-adjacent residues	884 – 885	2
	Non-terminal residue	902	1

Sequences

	Sequence		Length	Mass (Da)
	P85097 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 93540162AA633C66	FASTA	902	101,519
	10 20 30 40 50 60 FSPIDRYNDN HTQETYEDRE WENVYRSTHG VNCTGSCSWK DGIVTWEGQE LNYPTTGPDM 70 80 90 100 110 120 PDFEPRGASY SWYLYSANRG VLWSMWQEEL QNNESPLDAW KSSWQEVNEL IAASNVYTVK 130 140 150 160 170 180 TYGPDRVAGF SPIPAMSMVS YASGARTPDA HFFTEVRVVS VSPDFAESTK LCDLWLAPKQ 190 200 210 220 230 240 GTDAAMALAM GHVMLREFHL DNPSDYFLNY CRQYTDFPFL VTLSKQKGDQ FVADRAADLV 250 260 270 280 290 300 DALGQENNPE WKPVLWNENT NDFATPHGTM GSRGKWNLEQ RLEDEETGEK LSVLGIEDEI 310 320 330 340 350 360 GTVRLQLADG STALVTTVYD LTMANYGLER GLGGQEPKDF NDDVPFTPAW QEKITGVPRE 370 380 390 400 410 420 LIIQIAREFA DNADKTHGRA VLNLVLLVGA QGVNGGGWAH YVGQEKLRPA EGWQTIAMAK 430 440 450 460 470 480 HMNSTSYFYN HSSQWRYETV TAQELLSPMA DKYQHHGDYN VLAARMGWLP SAPQLGTNPL 490 500 510 520 530 540 RQAGMSPVDY TVKFAAEQPE NGKNHPRNLF VWRSNLLGSS GKGHEYMLKY LLGTENGIQG 550 560 570 580 590 600 KQGGVKPEEV EWKLSSTCLY SDIVLPTATW YEKDDMNTSD MHPFIHPLSA AVDPAWESKS 610 620 630 640 650 660 DWDIFTSLSK KFSEVCVGHL GKETDVVTLP IQHDSAAELA QPLDVKDWKG ECEPIPGKTM 670 680 690 700 710 720 PQIHVVERDY PATYERFTSI GPLMEKGIAW NTQSEMDLLR AWAALSEFTG RDHTHLALNK 730 740 750 760 770 780 EDEKFRDIQA QPRTVITSPA FTGSEKQSFY LDHDMMKDFG ESLLVYRPPI DTRKSRPEVE 790 800 810 820 830 840 GKEITLNYLT PHNKGGPIVW ISETDARDLG IEDNDWIEVF NSNGALTARV PAGMTMMYHA 850 860 870 880 890 900 QERGGIHNSV TRPTHMIGGY AQLAYGFNYY GTVGSNRDEF VVVRNINWLD GEGNDQVQES VK

References

[1]

"Identification of membrane-bound respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus) USDA 3045 by tandem mass spectrometry." Polcyn W. Submitted (FEB-2007) to UniProtKB Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION. Strain: USDA 3045.

Cross-references

3D structure databases
ProteinModelPortal	P85097.
SMR	P85097. Positions 2-900.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006655. Mopterin_OxRdtase_prok_CS. [Graphical view]
Pfam	PF00384. Molybdopterin. 2 hits. PF01568. Molydop_binding. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. Partial match. PS00490. MOLYBDOPTERIN_PROK_2. 1 hit. PS00932. MOLYBDOPTERIN_PROK_3. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NARG_BRASZ

Accession

Primary (citable) accession number: P85097

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program