A0A927JCB1 · A0A927JCB1_9ACTN

  • Protein
    assimilatory sulfite reductase (ferredoxin)
  • Gene
    nirB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per subunit.
siroheme (UniProtKB | Rhea| CHEBI:60052 )

Note: Binds 1 siroheme per subunit.

Pathway

Nitrogen metabolism; nitrate reduction (assimilation).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site635[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site641[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site675[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site679[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site679Fe (UniProtKB | ChEBI) of siroheme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular FunctionNADP binding
Molecular Functionoxidoreductase activity
Biological Processnitrate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    assimilatory sulfite reductase (ferredoxin)
  • EC number

Gene names

    • Name
      nirB
    • ORF names
      HT102_09140

Organism names

  • Taxonomic identifier
  • Strain
    • G463
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Hoyosellaceae > Lolliginicoccus

Accessions

  • Primary accession
    A0A927JCB1

Proteomes

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-285FAD/NAD(P)-binding
Domain322-387NADH-rubredoxin oxidoreductase C-terminal
Domain422-469BFD-like [2Fe-2S]-binding
Domain554-615Nitrite/Sulfite reductase ferredoxin-like
Domain626-751Nitrite/sulphite reductase 4Fe-4S

Sequence similarities

Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    843
  • Mass (Da)
    89,207
  • Last updated
    2023-02-22 v1
  • Checksum
    2046D16590F77B74
MMQKNIVVVGHGMVGHRFIEALRARDEQGEWKITVLCEEPVAAYDRVALSSYVSTWDHKELALSGNDYPGDTHVEVRLGERGEAIDPEARTVTTTRGDVIHYDKLVLATGSYAFVPPVPGKDAERCFVYRTLEDLDKIRAAAEASPAGAVGVVVGGGLLGLEAANALKLMGLTPHVVELAPRLMPLQVDEGGGAQLKSLVSDLGLTIHTGVSTAAIIEQQDGTLAVELSDGSVIDASLLVFSAGVRPRDELARTSGIDVGERGGIITDLSCRTSSEDIYAIGEVAAIEGRCYGLVGPGYATAEVVADRLLGGTAEFPGADLSTKLKLLGVDVASFGDAFATTPGALEVVLSNPAAGTYAKIVLSDDAKTLLGGILVGDASAYATLRPMVGRELPGDPAALIAPAGGGSAEIGTAALPDDAQICSCNAVTKGDICGAIDNGACDVASVKSCTKAGASCGGCLPLVKKLLADSGVELSKALCEHFSHSRQELFQIVQMTGIRTFSELIAKHGTGKGCDICKPTVASILASTSSEHILDGEQATLQDTNDHFLANLQKNGTYSVVPRMPGGEVTPDQLIVIGQIAKEFDLYVKVTGGQRIDMFGARVEQLPRIWQRLVDAGMESGHAYGKSLRTVKSCVGSSWCRYGQQDSVKMAVDLEKRYRGLRSPHKLKLAVSGCARECAEARGKDVGVIATERGWNLYVGGNGGQTPKHAVLLASDLDDETLIKYIDRYLMFYIRTADRLQRTAPWQESLDGGIDYVRQVVCEDSLGLADELEAAMEKHVAGYKDEWAGVLEDPEKLSRFVSFVNAPEEADPTVQFTESDGRKVPVGLGMPAMPATTTAGVK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACYWE010000004
EMBL· GenBank· DDBJ
MBD8506651.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp