I3R9M9 · NARG_HALMT

Function

function

The respiratory membrane-bound nitrate reductase enzyme complex plays a role in generation of metabolic energy by using nitrate as a terminal electron acceptor during anaerobic conditions. The alpha chain is the actual site of nitrate reduction.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per subunit.
Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | Rhea| CHEBI:60539 )

Note: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.

Activity regulation

Inhibited by cyanide, azide and antimycin A. Enzyme stability is not dependent on salt concentration.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.82 mMnitrate
0.25 mMmethyl viologen
Characterized with purified enzyme corresponding to a dimer of NarG and NarH.

pH Dependence

Optimum pH is 8.2. At 40 degrees Celsius (temperature of natural environment) the optimum pH is 7.9.

Temperature Dependence

Optimum temperature is 70 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site110[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site114[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site118[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site153[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site249Mo (UniProtKB | ChEBI) of Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionmetal ion binding
Molecular Functionmolybdopterin cofactor binding
Molecular Functionnitrate reductase (quinone) activity
Biological Processanaerobic respiration
Biological Processnitrate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Respiratory nitrate reductase subunit alpha
  • EC number
  • Alternative names
    • Nitrate reductase alpha chain

Gene names

    • Name
      narG
    • ORF names
      C439_00690
    • Ordered locus names
      HFX_5104

Encoded on

  • Plasmid pHM300

Organism names

Accessions

  • Primary accession
    I3R9M9
  • Secondary accessions
    • Q703H6

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, signal.

TypeIDPosition(s)Description
ChainPRO_0000428886?-984Respiratory nitrate reductase subunit alpha
Signal1-?Tat-type signal

Post-translational modification

Exported by the Tat system.

Expression

Induction

By nitrate.

Interaction

Subunit

Probable multiprotein complex; a catalytic heterodimer of an alpha and beta chain is proposed to associate with additional subunits involved in membrane attachment and electron transfer.

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-43Disordered
Compositional bias7-21Polar residues
Domain103-1674Fe-4S Mo/W bis-MGD-type

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    984
  • Mass (Da)
    111,326
  • Last updated
    2012-09-05 v1
  • Checksum
    4CECDC63C15F628E
MSRNDASQLDDGETTAESPPDDQANDAPEVGDPPGDPVDADSGVSRRTFLEGIGVASLLGIGTSAASDDSLFQMGGLKPVDDPIGNYPYRDWEDLYREKWDWDSVSRSTHSVNCTGSCSWNVYVKNGQVWREEQSGDYPRFDESLPDPNPRGCQKGACYTDYVNADQRIKHPLKRVGERGEGKWKRISWDEALTEIAEHVVDEVEAGRYDAISGFTPIPAMSPVSFASGSRLVNLLGGVSHSFYDWYSDLPPGQPITWGTQTDNAESADWYNADYIIAWGSNINVTRIPDAKYFLESGYNGTKRVGVFTDYSQTAIHTDEWLSPDSGTDTALALGMAQTIVDEGLYDEAHLKEQTDMPLLVRQDTGKFLRASDVPSVNTDADRPEWMLLMLDSNGRIREAPGSLGERDGQKDYSKSIELDFDPQLDGETTVQTQSGRVQVRTVWAELRDELANWDPEMVHEETTVGKETYQRIAREFAEADKAKIIQGKGVNDWYHNDLGNRALQLLVTLTGNLGEQGTGLDHYVGQEKIWTFHGWKTLSFPTGKVRGVPTTLWTYYHAGILDNTDPDTAAKIRESIDKGWMPVYPEERDNGSRPDPTTMFVWRGNYFNQAKGNVAVEEQLWPKLDLVVDINFRMDSTAMYSDIVLPTASHYEKHDLSMTDMHTYVHPFTPAVEPLGESKTDWQIFRELAQKIQEVATERGVEPISDRKFDREIDLQSVYDDYVRDWETGEEGALAEDRAACEYILEHSEESNPADSDEQITFADTVEQPQRLLEAGDHWTSDIEDGEAYAPWKDFVQDKNPWPTVTGRQQYYIDHDWFLELGEELPTHKEGPENTGGDYPMEYNTPHGRWAIHSTWRDSEKLLRLQRGEPLLYLHPEDAEERGIEDGDSVEVFNDLAEVELQAKIYPSSQRGTARMYFAWERFQFDSDSNFNSLVPMYMKPTQLVQYPEDSGEHLHFFPNYWGPTGVNSDVRVDVRKAGGGDE

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias7-21Polar residues
Sequence conflict281-282in Ref. 1; CAF21906
Sequence conflict429-434in Ref. 1; CAF21906
Sequence conflict564-566in Ref. 1; CAF21906
Sequence conflict603in Ref. 1; CAF21906
Sequence conflict694in Ref. 1; CAF21906
Sequence conflict709in Ref. 1; CAF21906
Sequence conflict833in Ref. 1; CAF21906

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ621880
EMBL· GenBank· DDBJ
CAF21906.1
EMBL· GenBank· DDBJ
Genomic DNA
CP001870
EMBL· GenBank· DDBJ
AFK20939.1
EMBL· GenBank· DDBJ
Genomic DNA
AOLO01000001
EMBL· GenBank· DDBJ
EMA05271.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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