A0A9Q5WQM4 · A0A9Q5WQM4_RHOHA

Function

function

Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source.

Miscellaneous

The a and c carboxylates of hydrogenobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CobB catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.

Caution

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

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 9/10.

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site343Nucleophile
Site441Increases nucleophilicity of active site Cys

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncobyrinic acid a,c-diamide synthase activity
Molecular Functionhydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) activity
Biological Processcobalamin biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hydrogenobyrinate a,c-diamide synthase
  • EC number
  • Alternative names
    • Hydrogenobyrinic acid a,c-diamide synthase

Gene names

    • Name
      cobB
    • ORF names
      B0F69_17330
      , GS882_25555
      , GS947_12705

Organism names

Accessions

  • Primary accession
    A0A9Q5WQM4

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-200CobQ/CobB/MinD/ParA nucleotide binding
Domain279-443CobB/CobQ-like glutamine amidotransferase

Domain

Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and hydrogenobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.

Sequence similarities

Belongs to the CobB/CbiA family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    460
  • Mass (Da)
    46,991
  • Last updated
    2023-09-13 v1
  • Checksum
    E20F2B56E6E0C5C8
MVNAPSTPAVVIAAPASGSGKTTVATGLVGALRAAGDRVAPFKVGPDYIDPGYHALAAGLPGRNLDSVLVGADRIGPLFRHGGDDCDIAVVEGVMGLFDGKIDPSSSAPSAEGSTAQVAAALGAPVVLVIDARGHSQSLAAVLHGFSTYDSAVRIGGVILNRVGSARHEQVLRQACERVGLPVLGAVPRLAELEVPSRHLGLVPAVEHGRAALDAVAAMTELAAAHLDLDAIRGLAHSSVGDVAWDPAAEIGPVPSGPRPVIALAGGVAFTFGYAEHRELLDAAGADVVVFDPLHDELPAGTAGLVLPGGFPEEHAVALSANRVLLQQVRQLAADGAPIHAECAGLLYLTRSLDGHAMAGVIDVDARFGKRLTLGYREAVAVTDSVLFGAGTRVTGHEFHRTALDAGVADGFGPAWGWRAWDAGATREGFTAGSVHASYLHTHPAGNPDAIRRFVEAARG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MULT01000006
EMBL· GenBank· DDBJ
MBP0098439.1
EMBL· GenBank· DDBJ
Genomic DNA
WVBC01000034
EMBL· GenBank· DDBJ
NKT81441.1
EMBL· GenBank· DDBJ
Genomic DNA
WVDC01000005
EMBL· GenBank· DDBJ
NKW42447.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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