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Protein

Cobyrinate a,c-diamide synthase

Gene

cbiA

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

2 ATP + cobyrinate + 2 L-glutamine + 2 H2O = 2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Pathwayi: adenosylcobalamin biosynthesis

This protein is involved in step 10 of the subpathway that synthesizes cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route).UniRule annotation
Proteins known to be involved in the 10 steps of the subpathway in this organism are:
  1. Sirohydrochlorin cobaltochelatase (cbiX)
  2. no protein annotated in this organism
  3. Cobalamin biosynthesis protein CbiHC (cbiHC)
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Cobalt-precorrin-5B C(1)-methyltransferase (cbiD)
  7. no protein annotated in this organism
  8. Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (cbiT)
  9. Cobalamin biosynthesis protein CbiHC (cbiHC)
  10. Cobyrinate a,c-diamide synthase (cbiA)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route), the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei335 – 3351NucleophileUniRule annotation
Sitei437 – 4371Increases nucleophilicity of active site CysUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cobalamin biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-2276-MONOMER.
UniPathwayiUPA00148; UER00231.

Names & Taxonomyi

Protein namesi
Recommended name:
Cobyrinate a,c-diamide synthaseUniRule annotation (EC:6.3.5.11UniRule annotation)
Alternative name(s):
Cobyrinic acid a,c-diamide synthetaseUniRule annotation
Gene namesi
Name:cbiAUniRule annotation
Ordered Locus Names:AF_2229
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Cobyrinate a,c-diamide synthasePRO_0000141273Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224325.AF2229.

Structurei

3D structure databases

ProteinModelPortaliO28054.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini254 – 445192GATase cobBQ-typeUniRule annotationAdd
BLAST

Domaini

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 cobyrinate 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.UniRule annotation

Sequence similaritiesi

Belongs to the CobB/CbiA family.UniRule annotation
Contains 1 GATase cobBQ-type domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiarCOG00106. Archaea.
COG1797. LUCA.
KOiK02224.
OMAiYIHLHVL.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00027. CobB_CbiA. 1 hit.
InterProiIPR004484. CbiA_synth.
IPR029062. Class_I_gatase-like.
IPR017929. CobB/CobQ_GATase.
IPR002586. CobQ/CobB/MinD/ParA_Nub-bd_dom.
IPR011698. GATase_3.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01656. CbiA. 1 hit.
PF07685. GATase_3. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00379. cobB. 1 hit.
PROSITEiPS51274. GATASE_COBBQ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O28054-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLPMDIPR VVIAGTSSKV GKTMISIGLM RLLVNRGYEV QPYKVGPDFI
60 70 80 90 100
DPGFHHLATG RYSRNLDSFM LSRSAILETF IRNFRGADVA IIEGKTGLYD
110 120 130 140 150
SSDAVSEKGS VAEVSKILKA PVVLVANVER LNRTAAAIIL GYKLFDPDVL
160 170 180 190 200
LKGVILNRVG SERHAGKVRT AVEKLAGVRV LGVVPRKKVK MPYRHLGLVT
210 220 230 240 250
AYEREDMDEL LDNIAEIVEK HVDVDKILEI AEKAPPLDSV FEDEKEDEEK
260 270 280 290 300
KYVKIGVIRD QVFSFYYQDN LDELSKYAEL VFVNSLTDKR LPDVDALYIG
310 320 330 340 350
GGFPEVFAEG LEKNEKLRNE IYDFCQSGNP VYAECGGLMY LGESLETSEG
360 370 380 390 400
EFEMVGFLPL KTKMYERFQA QGYSVYRTLK PCIIAKRNQK IVGHEFHYSR
410 420 430 440 450
PTLTGKADFA FRVERGFGID GRRDGILKEN TLGCYIHVHF LSDKSIARRF

VKKAMKKK
Length:458
Mass (Da):51,628
Last modified:January 1, 1998 - v1
Checksum:iAE6F2E0DD5713C13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89025.1.
PIRiE69528.

Genome annotation databases

EnsemblBacteriaiAAB89025; AAB89025; AF_2229.
KEGGiafu:AF_2229.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89025.1.
PIRiE69528.

3D structure databases

ProteinModelPortaliO28054.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF2229.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB89025; AAB89025; AF_2229.
KEGGiafu:AF_2229.

Phylogenomic databases

eggNOGiarCOG00106. Archaea.
COG1797. LUCA.
KOiK02224.
OMAiYIHLHVL.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00231.
BioCyciAFUL224325:GJBC-2276-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00027. CobB_CbiA. 1 hit.
InterProiIPR004484. CbiA_synth.
IPR029062. Class_I_gatase-like.
IPR017929. CobB/CobQ_GATase.
IPR002586. CobQ/CobB/MinD/ParA_Nub-bd_dom.
IPR011698. GATase_3.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01656. CbiA. 1 hit.
PF07685. GATase_3. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00379. cobB. 1 hit.
PROSITEiPS51274. GATASE_COBBQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBIA_ARCFU
AccessioniPrimary (citable) accession number: O28054
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.