A0A6I3S9G5 · A0A6I3S9G5_9BURK

Function

function

Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process.

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:
Cu+ (UniProtKB | Rhea| CHEBI:49552 )

Note: Exposure to oxygen reduces copper binding and leads to the formation of a disulfide bond between the two Cys residues that bind the copper ion.
heme c (UniProtKB | Rhea| CHEBI:61717 )

Note: Binds 8 heme c groups covalently per monomer.

Pathway

Sulfur metabolism; sulfite reduction.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site145heme c 1 (UniProtKB | ChEBI); covalent
Binding site148heme c 1 (UniProtKB | ChEBI); covalent
Binding site149Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue
Binding site161Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue
Binding site209substrate
Binding site286substrate
Binding site303heme c 2 (UniProtKB | ChEBI); covalent
Binding site306heme c 2 (UniProtKB | ChEBI); covalent
Binding site307Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue
Binding site340heme c 3 (UniProtKB | ChEBI); covalent
Binding site343heme c 3 (UniProtKB | ChEBI); covalent
Binding site344Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue
Binding site349Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue
Binding site361heme c 4 (UniProtKB | ChEBI); covalent
Binding site364heme c 4 (UniProtKB | ChEBI); covalent
Binding site365Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue
Binding site367substrate
Binding site399Cu+ (UniProtKB | ChEBI)
Binding site411Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue
Binding site418heme c 5 (UniProtKB | ChEBI); covalent
Binding site421heme c 5 (UniProtKB | ChEBI); covalent
Binding site422Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue
Binding site425Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue
Binding site445heme c 6 (UniProtKB | ChEBI); covalent
Binding site448heme c 6 (UniProtKB | ChEBI); covalent
Binding site449Fe (UniProtKB | ChEBI) of heme c 6 (UniProtKB | ChEBI); axial binding residue
Binding site462Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue
Binding site467heme c 7 (UniProtKB | ChEBI); covalent
Binding site470heme c 7 (UniProtKB | ChEBI); covalent
Binding site471Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue
Binding site478Cu+ (UniProtKB | ChEBI)
Binding site499Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue
Binding site545heme c 8 (UniProtKB | ChEBI); covalent
Binding site561heme c 8 (UniProtKB | ChEBI); covalent
Binding site562Fe (UniProtKB | ChEBI) of heme c 8 (UniProtKB | ChEBI); axial binding residue
Binding site646Fe (UniProtKB | ChEBI) of heme c 7 (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentperiplasmic space
Molecular Functioncopper ion binding
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionsulfite reductase activity
Biological Processanaerobic respiration
Biological Processhydrogen sulfide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dissimilatory sulfite reductase
  • EC number

Gene names

    • ORF names
      GMD42_08560

Organism names

  • Taxonomic identifier
  • Strain
    • BIOML-A2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Sutterellaceae > Parasutterella

Accessions

  • Primary accession
    A0A6I3S9G5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_503168057726-681Dissimilatory sulfite reductase

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain144-166Cytochrome c-552/4
Domain415-453Doubled CXXCH motif

Sequence similarities

Belongs to the multiheme cytochrome c family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    681
  • Mass (Da)
    76,173
  • Last updated
    2020-08-12 v1
  • Checksum
    C569DB90891543CD
MLRETRKTAIGLGLAAAMATSCVYAADGQPLPTPKVNEITQKVWANPDLTEPTKGIRTLQDYIVQEKELWDFLFQNHPIFATYGKDGRVIGTPVISTRGSEYLGEGNAQKYSAHQDGNRPMASQYRLGQRSILDFPNKFVGPEKCGECHAIQYEQWKRSRHAKTVRFPGEHPEVDNDLKKKLYGSEASILPDGITADVIYATIGTPRTKYGYIDGWLVRGSYHVRDGLLKDGTGKVVAGGNQFSRGWAEWLTPEKAKEIQKLIPDFPTELSQFGPSASHQWGMTSYGSTYEGKLLFQAASSYCEVCHAFKFDFKDKKEFFAALGNPKELQKHTISRGIACEECHGEGGHLVGNTNNMSTNCDRCHQRLNFIEDEVDRPDAKGKLEKAFNAKTKSSCPSCGTEGAQLFMSKHYEKGMRCVTCHDPHEVTSNDWTSGVTRPAIRKNCQDCHTTQAQMVANADTHSKVDCIACHMPFTMSCENFTAIQRPDMAGFDAVRRSHLFKIMVDPDKKMMNPGPGQSRASNSKGWRISRDEEGHGYVDLMWSCARTSIADFTVVEGKGCHSPFQSELDQGLIYQDQKEIYGEVMKWQNPIKEGHQKNVEALTRINKLLEVTKLTPEQRTEAMLLIDKAGEIIKQVQDDGSWGVHAFNYTKQRVETAQAYLTKAQSIIDQGGYKAVKATK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WNCL01000025
EMBL· GenBank· DDBJ
MTU43671.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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