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UniProtKB - Q9ZB63 (CARY_GEOSE)

Entry version 94 (02 Dec 2020)
Sequence version 1 (01 May 1999)
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Protein

Carbamoyl-phosphate synthase arginine-specific large chain

Gene

carB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score:

Annotation score:4 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+By similarity, Mn2+By similarityNote: Binds 4 Mg2+ or Mn2+ ions per subunit.By similarity

<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>Temperature dependencei

Thermostable up to 63 degrees Celsius.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase arginine-specific small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase arginine-specific large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from bicarbonate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi285Magnesium or manganese 1By similarity1
Metal bindingi299Magnesium or manganese 1By similarity1
Metal bindingi299Magnesium or manganese 2By similarity1
Metal bindingi301Magnesium or manganese 2By similarity1
Metal bindingi822Magnesium or manganese 3By similarity1
Metal bindingi834Magnesium or manganese 3By similarity1
Metal bindingi834Magnesium or manganese 4By similarity1
Metal bindingi836Magnesium or manganese 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi160 – 217ATPBy similarityAdd BLAST58
Nucleotide bindingi702 – 756ATPBy similarityAdd BLAST55

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 processAmino-acid biosynthesis, Arginine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9ZB63

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

More...UniPathwayi		UPA00068;UER00171

<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%5Fand%5Ftaxonomy%5Fsection">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:
Carbamoyl-phosphate synthase arginine-specific large chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:carB
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1422 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001449901 – 1043Carbamoyl-phosphate synthase arginine-specific large chainAdd BLAST1043

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9ZB63

Database of comparative protein structure models

More...ModBasei		Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini134 – 328ATP-grasp 1Add BLAST195
Domaini676 – 863ATP-grasp 2Add BLAST188
Domaini930 – 1037MGS-likePROSITE-ProRule annotationAdd BLAST108

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 402Carboxyphosphate synthetic domainAdd BLAST402
Regioni403 – 550Oligomerization domainAdd BLAST148
Regioni551 – 932Carbamoyl phosphate synthetic domainAdd BLAST382
Regioni933 – 1043Allosteric domainAdd BLAST111

<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 CarB family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1030.10, 1 hit
3.30.1490.20, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01210_B, CPSase_L_chain_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR006275, CarbamoylP_synth_lsu
IPR005480, CarbamoylP_synth_lsu_oligo
IPR036897, CarbamoylP_synth_lsu_oligo_sf
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR005483, CbamoylP_synth_lsu_CPSase_dom
IPR011607, MGS-like_dom
IPR016185, PreATP-grasp_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02786, CPSase_L_D2, 2 hits
PF02787, CPSase_L_D3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00098, CPSASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01096, CPSase_L_D3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48108, SSF48108, 1 hit
SSF52440, SSF52440, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01369, CPSaseII_lrg, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50975, ATP_GRASP, 2 hits
PS00866, CPSASE_1, 2 hits
PS00867, CPSASE_2, 2 hits
PS51855, MGS, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9ZB63-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKDSSLQSI LLIGSGRSSS AKAAEFDYSG TQACIAFKEE GYRVILVNNN 
        60         70         80         90        100
PATIMTDDVH ADAVYFEPLT VEAVEAIIAK ETPDGLLATF GGQTGLNLAF 
       110        120        130        140        150
QLHEAGVLKK YGVRLLGTPI EAIKRPRGGP RTFRALMHEL GEPVPESEIV 
       160        170        180        190        200
TSVEEAVAFA EQIGFPIIIR PAYTLGGTGG GIAENMEQFL ALVEKGLNES 
       210        220        230        240        250
PIHQCLIERS VAGFKEIEYE VMRDQSNTCI TVCNMENVDP VGIHTGDSIV 
       260        270        280        290        300
VAPSQTLTDE EYQMLRSSAV KIISALGIIG GCNIQFALDP NSKQYYLIEV 
       310        320        330        340        350
NPRVSRSSAL ASKATGYPIA ALPAKLAVGY TLAELVNPVT KTTYASFEPA 
       360        370        380        390        400
LDYVVVKFPR LPFDKFPHAD RKLGTQMKAT GEVMAIDRNM ERAFQKAVQS 
       410        420        430        440        450
LEGKNNGLLL PELSVKTNDE LKQLLVDKDD RRFFAILELL RRGVAVEAIH 
       460        470        480        490        500
KWTKIDRFFL CSFERLVALE KQAAAATLDT IEEQTFRFLK EKGCSDAFLA 
       510        520        530        540        550
ETWGVTELDV RNKRKELGIV PSYKMVDTCA AEFHSETDYY YSTYFGEDER 
       560        570        580        590        600
KQPSGKEKVL IIGAGPIRIG QGIEFDYSSV HSVFALQKEG YETVMINNNP 
       610        620        630        640        650
ETVSTDFAVA DRLYFEPLTL ESVLDVIEAE QIKHVIVQFG GQTAINLVKG 
       660        670        680        690        700
LEEAGVPLLG VTYDMIDQLE DRDRFYQLLE ELDIPHVPGL VANNAEELAA 
       710        720        730        740        750
KAAEIGYPVL LRPSYVIGGC GMFIVHSEAQ LAALIEQGEL TYPILIDAYL 
       760        770        780        790        800
DGKEAEADIV TDGTDIVLPV IIEHVEKAGV HSGDSYAWLP AQTLTGEEKA 
       810        820        830        840        850
KIIDYAGRIA KKLGFKGIMN IQYVIADGNV YVLEVNPRAS RTVPIVSKTT 
       860        870        880        890        900
GVPLAQIATK LLLGKSLVDI VDEKARGLAV MPYAVLKYPV FSTHKLPGVD 
       910        920        930        940        950
PMVGPEMKST GEGISIAATK EEAAYKAFYP YLQKKANANE VYVIGNIDAE 
       960        970        980        990       1000
LEAEMTAKQL TIVADVPFSD WVKRDTALAV IDLGKEEGEA NKRMTALSRQ 
      1010       1020       1030       1040 
LLVFTERETL KLFLQALDVD HLDVQPIHGW LEKKKQAEQA VIA
Length:1,043
Mass (Da):114,522
Last modified:May 1, 1999 - v1
<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:iE97E7334E70B4C11
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
U43091 Genomic DNA Translation: AAC78719.1

<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
U43091 Genomic DNA Translation: AAC78719.1

3D structure databases

SMRiQ9ZB63
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00068;UER00171
SABIO-RKiQ9ZB63

Family and domain databases

Gene3Di1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
HAMAPiMF_01210_B, CPSase_L_chain_B, 1 hit
InterProiView protein in InterPro
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR006275, CarbamoylP_synth_lsu
IPR005480, CarbamoylP_synth_lsu_oligo
IPR036897, CarbamoylP_synth_lsu_oligo_sf
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR005483, CbamoylP_synth_lsu_CPSase_dom
IPR011607, MGS-like_dom
IPR016185, PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF02786, CPSase_L_D2, 2 hits
PF02787, CPSase_L_D3, 1 hit
PRINTSiPR00098, CPSASE
SMARTiView protein in SMART
SM01096, CPSase_L_D3, 1 hit
SUPFAMiSSF48108, SSF48108, 1 hit
SSF52440, SSF52440, 2 hits
TIGRFAMsiTIGR01369, CPSaseII_lrg, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 2 hits
PS00866, CPSASE_1, 2 hits
PS00867, CPSASE_2, 2 hits
PS51855, MGS, 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 nameiCARY_GEOSE
<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: Q9ZB63
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: May 1, 1999
Last modified: December 2, 2020
This is version 94 of the entry and version 1 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

Documents

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