Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 88 (08 May 2019)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Hydrogenobyrinate a,c-diamide synthase

Gene

cobB

Organism
Sinorhizobium sp.
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. To a much lesser extent, can also use cobyrinate as substrate in vitro, but the physiological substrate is indeed hydrogenobyrinate, as part of the aerobic pathway for cobalamin biosynthesis.UniRule annotationCurated1 Publication

Miscellaneous

The a and c carboxylates of hydrogenobyrinate are likely 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 annotation1 Publication

Caution

Was originally thought to originate from Pseudomonas denitrificans, but similarity searches show that the sequence is much closer to Sinorhizobium. The entry's taxonomy has been changed.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.41 µM for hydrogenobyrinate1 Publication
  2. KM=0.21 µM for hydrogenobyrinate c-monoamide1 Publication
  3. KM=30.2 µM for ATP1 Publication
  4. KM=20.3 µM for glutamine1 Publication
  5. KM=12 mM for ammonia1 Publication
  6. KM=250 µM for cobyrinate1 Publication
  1. Vmax=1390 nmol/h/mg enzyme with hydrogenobyrinate as substrate1 Publication
  2. Vmax=574 nmol/h/mg enzyme with hydrogenobyrinate c-monoamide as substrate1 Publication
  3. Vmax=800 nmol/h/mg enzyme with cobyrinate as substrate1 Publication

pH dependencei

Optimum pH is around 7.3.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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 annotationCurated
Proteins known to be involved in the 10 steps of the subpathway in this organism are:
  1. Precorrin-2 C(20)-methyltransferase (cobI)
  2. Precorrin-3B synthase (cobG)
  3. Precorrin-3B C(17)-methyltransferase (cobJ)
  4. Precorrin-4 C(11)-methyltransferase (cobM)
  5. Precorrin-6A synthase [deacetylating] (cobF)
  6. Precorrin-6A reductase (cobK)
  7. Precorrin-6Y C(5,15)-methyltransferase [decarboxylating] (cobL)
  8. Precorrin-8X methylmutase (cobH)
  9. Hydrogenobyrinate a,c-diamide synthase (cobB)
  10. Aerobic cobaltochelatase subunit CobT (cobT), Aerobic cobaltochelatase subunit CobS (cobS), Aerobic cobaltochelatase subunit CobN (cobN)
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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei326NucleophileUniRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei426Increases nucleophilicity of active site CysUniRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-116

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P21632

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00148;UER00220

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Hydrogenobyrinate a,c-diamide synthaseUniRule annotation1 Publication (EC:6.3.5.9UniRule annotation1 Publication)
Alternative name(s):
Hydrogenobyrinic acid a,c-diamide synthaseUniRule annotation1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cobB1 PublicationUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSinorhizobium sp.
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri42445 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001412652 – 434Hydrogenobyrinate a,c-diamide synthaseAdd BLAST433

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini243 – 434GATase cobBQ-typeUniRule annotationAdd BLAST192

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the CobB/CbiA family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.880, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00027 CobB_CbiA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004484 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

The PANTHER Classification System

More...
PANTHERi
PTHR43873 PTHR43873, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01656 CbiA, 1 hit
PF07685 GATase_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52317 SSF52317, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00379 cobB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51274 GATASE_COBBQ, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P21632-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGLLIAAPA SGSGKTTVTL GLMRALKRRG VAIAPGKAGP DYIDPAFHAA
60 70 80 90 100
ATGEPCFNYD PWAMRPELLL ANASHVASGG RTLIVEAMMG LHDGAADGSG
110 120 130 140 150
TPADLAATLN LAVILVVDCA RMSQSVAALV RGYADHRDDI RVVGVILNKV
160 170 180 190 200
GSDRHEMMLR DALGKVRMPV FGVLRQDSAL QLPERHLGLV QAGEHSALEG
210 220 230 240 250
FIEAAAARVE AACDLDAIRL IATIFPQVPA AADAERLRPL GQRIAVARDI
260 270 280 290 300
AFAFCYEHLL YGWRQGGAEI SFFSPLADEG PDAAADAVYL PGGYPELHAG
310 320 330 340 350
QLSAAARFRS GMHSAAERGA RIFGECGGYM VLGEGLVAAD GTRYDMLGLL
360 370 380 390 400
PLVTSFAERR RHLGYRRVVP VDNAFFDGPM TAHEFHYATI VAEGAADRLF
410 420 430
AVSDAAGEDL GQAGLRRGPV AGSFMHLIDV AGAA
Length:434
Mass (Da):45,705
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDE3D15D099BC0BCA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M59236 Genomic DNA Translation: AAA25774.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59236 Genomic DNA Translation: AAA25774.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Enzyme and pathway databases

UniPathwayiUPA00148;UER00220
BioCyciMetaCyc:MONOMER-116
SABIO-RKiP21632

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
IPR002586 CobQ/CobB/MinD/ParA_Nub-bd_dom
IPR011698 GATase_3
IPR027417 P-loop_NTPase
PANTHERiPTHR43873 PTHR43873, 1 hit
PfamiView protein in Pfam
PF01656 CbiA, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCOBB_SINSX
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21632
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 88 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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.

Do not show this banner again