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Protein

Hydrogenobyrinate a,c-diamide synthase

Gene

cobB

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Pathwayi: adenosylcobalamin biosynthesis

This protein is involved in step 9 of the subpathway that synthesizes cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route).UniRule annotation
Proteins known to be involved in the 10 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
  7. no protein annotated in this organism
  8. no protein annotated in this organism
  9. Hydrogenobyrinate a,c-diamide synthase (cobB)
  10. no protein annotated in this organism
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 precorrin-2 (aerobic route), the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei327NucleophileUniRule annotation1
Sitei427Increases nucleophilicity of active site CysUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processCobalamin biosynthesis
LigandATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00148; UER00220

Names & Taxonomyi

Protein namesi
Recommended name:
Hydrogenobyrinate a,c-diamide synthaseUniRule annotation (EC:6.3.5.9UniRule annotation)
Alternative name(s):
Hydrogenobyrinic acid a,c-diamide synthaseUniRule annotation
Gene namesi
Name:cobBUniRule annotation
Ordered Locus Names:BMEI0705
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001412551 – 436Hydrogenobyrinate a,c-diamide synthaseAdd BLAST436

Interactioni

Protein-protein interaction databases

STRINGi224914.BAWG_2678

Structurei

3D structure databases

ProteinModelPortaliQ8YHU1
SMRiQ8YHU1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini244 – 435GATase cobBQ-typeUniRule annotationAdd BLAST192

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 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.UniRule annotation

Sequence similaritiesi

Belongs to the CobB/CbiA family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105C0Y Bacteria
COG1797 LUCA
HOGENOMiHOG000289959
KOiK02224
OMAiQPFKCGP

Family and domain databases

Gene3Di3.40.50.880, 1 hit
HAMAPiMF_00027 CobB_CbiA, 1 hit
InterProiView protein in InterPro
IPR004484 CbiA_synth
IPR029062 Class_I_gatase-like
IPR017929 CobB/CobQ_GATase
IPR011698 GATase_3
IPR027417 P-loop_NTPase
PANTHERiPTHR43873 PTHR43873, 1 hit
PfamiView protein in Pfam
PF07685 GATase_3, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00379 cobB, 1 hit
PROSITEiView protein in PROSITE
PS51274 GATASE_COBBQ, 1 hit

Sequencei

Sequence statusi: Complete.

Q8YHU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGFMIAAPA SGSGKTTVTL GLLRALKRRG EVLAPVKAGP DYIDPAYHRA
60 70 80 90 100
ASGVDCFNLD PWAMRPELIS ALSSRMTESG ARVLVAEGMM GLFDGAIDGK
110 120 130 140 150
GSSADLARLL DLPVVLVVDC ARQSHSIAAL VWGFSQFRKD VLIEGVILNR
160 170 180 190 200
VGSPRHEAML RGALAPLGVP VLGALPRDPA LSLPERHLGL VQADEHAGLE
210 220 230 240 250
SFLEQAADVM EAHIDMDALQ TIWLRPKRYD AMANVARLKP LGNRIAVARD
260 270 280 290 300
DAFAFAYMHL FEGWRRRGAE ISFFSPLADE APKADADAIY LPGGYPELHA
310 320 330 340 350
QRLAGASRFR TAIGDAAARG VTVYGECGGY MVLGKTLEDA AGVHHPMLGL
360 370 380 390 400
LPLETSFARR KLHLGYRLLE PLGGLPWDMP LKAHEFHYAS IVREEKADRL
410 420 430
FRVRDASGEN LGEAGLRVGS VSGSFMHVID FSGEAA
Length:436
Mass (Da):47,034
Last modified:March 1, 2002 - v1
Checksum:iAED85D8A1549862B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA Translation: AAL51886.1
PIRiAC3340
RefSeqiWP_002964414.1, NZ_GG703780.1

Genome annotation databases

EnsemblBacteriaiAAL51886; AAL51886; BMEI0705
GeneIDi29593498
KEGGibme:BMEI0705
bmel:DK63_722
PATRICifig|224914.52.peg.755

Entry informationi

Entry nameiCOBB_BRUME
AccessioniPrimary (citable) accession number: Q8YHU1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2002
Last modified: June 7, 2017
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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