Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ornithine carbamoyltransferase, catabolic

Gene

arcB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.1 Publication

Catalytic activityi

Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.

Enzyme regulationi

Inhibited by 2-aminopentanoic acid (norvaline).1 Publication

Kineticsi

  1. KM=0.32 mM for carbamoyl phosphate (at pH 6.8 and 37 degrees Celsius)1 Publication
  2. KM=0.22 mM for L-ornithine (at pH 6.8 and 37 degrees Celsius)1 Publication

    Pathwayi: L-arginine degradation via ADI pathway

    This protein is involved in step 2 of the subpathway that synthesizes carbamoyl phosphate from L-arginine.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Arginine deiminase (arcA)
    2. Ornithine carbamoyltransferase, catabolic (arcB)
    This subpathway is part of the pathway L-arginine degradation via ADI pathway, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from L-arginine, the pathway L-arginine degradation via ADI pathway and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei33Carbamoyl phosphate1
    Binding sitei73Carbamoyl phosphateBy similarity1
    Binding sitei84Carbamoyl phosphateBy similarity1
    Binding sitei108Carbamoyl phosphateBy similarity1
    Binding sitei168OrnithineBy similarity1
    Binding sitei232OrnithineBy similarity1
    Binding sitei303Carbamoyl phosphateBy similarity1
    Binding sitei321Carbamoyl phosphateBy similarity1

    GO - Molecular functioni

    • amino acid binding Source: InterPro
    • ornithine carbamoyltransferase activity Source: PseudoCAP

    GO - Biological processi

    • arginine biosynthetic process via ornithine Source: GO_Central
    • arginine catabolic process to ornithine Source: UniProtKB-UniPathway
    • arginine deiminase pathway Source: PseudoCAP
    • urea cycle Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Arginine metabolism

    Enzyme and pathway databases

    SABIO-RKP08308.
    UniPathwayiUPA00254; UER00365.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine carbamoyltransferase, catabolic (EC:2.1.3.3)
    Short name:
    OTCase
    Gene namesi
    Name:arcB
    Ordered Locus Names:PA5172
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA5172.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi106E → A or G: Loss of homotropic cooperativity; gain of anabolic activity. Conformational change which modifies the catalytic site. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00001129862 – 336Ornithine carbamoyltransferase, catabolicAdd BLAST335

    Proteomic databases

    PaxDbiP08308.
    PRIDEiP08308.

    Interactioni

    Subunit structurei

    Dodecamer (tetramer of trimers).2 Publications

    Protein-protein interaction databases

    STRINGi208964.PA5172.

    Structurei

    Secondary structure

    1336
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 13Combined sources4
    Helixi18 – 36Combined sources19
    Beta strandi48 – 55Combined sources8
    Helixi58 – 70Combined sources13
    Beta strandi74 – 78Combined sources5
    Turni80 – 82Combined sources3
    Turni85 – 87Combined sources3
    Helixi91 – 101Combined sources11
    Beta strandi103 – 108Combined sources6
    Helixi112 – 121Combined sources10
    Beta strandi122 – 124Combined sources3
    Beta strandi126 – 130Combined sources5
    Helixi136 – 148Combined sources13
    Helixi154 – 156Combined sources3
    Beta strandi158 – 163Combined sources6
    Helixi168 – 179Combined sources12
    Beta strandi183 – 187Combined sources5
    Helixi190 – 192Combined sources3
    Helixi196 – 209Combined sources14
    Beta strandi212 – 217Combined sources6
    Helixi219 – 222Combined sources4
    Turni223 – 225Combined sources3
    Beta strandi227 – 231Combined sources5
    Beta strandi237 – 239Combined sources3
    Helixi241 – 243Combined sources3
    Helixi245 – 251Combined sources7
    Helixi252 – 254Combined sources3
    Helixi258 – 262Combined sources5
    Beta strandi270 – 273Combined sources4
    Beta strandi280 – 283Combined sources4
    Helixi284 – 292Combined sources9
    Helixi294 – 298Combined sources5
    Beta strandi299 – 303Combined sources5
    Helixi304 – 307Combined sources4
    Beta strandi309 – 312Combined sources4
    Helixi314 – 333Combined sources20

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei32Important for structural integrity1
    Sitei148Important for structural integrity1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1DXHX-ray2.50A2-336[»]
    1ORTX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L2-336[»]
    ProteinModelPortaliP08308.
    SMRiP08308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08308.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni11 – 16Carbamoyl phosphate binding6
    Regioni57 – 61Carbamoyl phosphate bindingBy similarity5
    Regioni135 – 138Carbamoyl phosphate bindingBy similarity4
    Regioni236 – 237Ornithine bindingBy similarity2
    Regioni273 – 276Carbamoyl phosphate bindingBy similarity4

    Sequence similaritiesi

    Belongs to the ATCase/OTCase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105DBV. Bacteria.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    InParanoidiP08308.
    KOiK00611.
    OMAiMGMEIRL.
    PhylomeDBiP08308.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_01109. OTCase. 1 hit.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    IPR024904. OTCase_ArgI.
    [Graphical view]
    PfamiPF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view]
    PRINTSiPR00100. AOTCASE.
    PR00102. OTCASE.
    SUPFAMiSSF53671. SSF53671. 1 hit.
    TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
    PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08308-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAFNMHNRNL LSLMHHSTRE LRYLLDLSRD LKRAKYTGTE QQHLKRKNIA
    60 70 80 90 100
    LIFEKTSTRT RCAFEVAAYD QGANVTYIDP NSSQIGHKES MKDTARVLGR
    110 120 130 140 150
    MYDAIEYRGF KQEIVEELAK FAGVPVFNGL TDEYHPTQML ADVLTMREHS
    160 170 180 190 200
    DKPLHDISYA YLGDARNNMG NSLLLIGAKL GMDVRIAAPK ALWPHDEFVA
    210 220 230 240 250
    QCKKFAEESG AKLTLTEDPK EAVKGVDFVH TDVWVSMGEP VEAWGERIKE
    260 270 280 290 300
    LLPYQVNMEI MKATGNPRAK FMHCLPAFHN SETKVGKQIA EQYPNLANGI
    310 320 330
    EVTEDVFESP YNIAFEQAEN RMHTIKAILV STLADI
    Length:336
    Mass (Da):38,109
    Last modified:January 23, 2007 - v3
    Checksum:i4E780414EADA4724
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05637 Genomic DNA. Translation: CAA29124.1.
    AE004091 Genomic DNA. Translation: AAG08557.1.
    PIRiS00032. OWPSCA.
    RefSeqiNP_253859.1. NC_002516.2.
    WP_003100031.1. NZ_ASJY01000811.1.

    Genome annotation databases

    EnsemblBacteriaiAAG08557; AAG08557; PA5172.
    GeneIDi881792.
    KEGGipae:PA5172.
    PATRICi19845187. VBIPseAer58763_5420.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05637 Genomic DNA. Translation: CAA29124.1.
    AE004091 Genomic DNA. Translation: AAG08557.1.
    PIRiS00032. OWPSCA.
    RefSeqiNP_253859.1. NC_002516.2.
    WP_003100031.1. NZ_ASJY01000811.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1DXHX-ray2.50A2-336[»]
    1ORTX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L2-336[»]
    ProteinModelPortaliP08308.
    SMRiP08308.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA5172.

    Proteomic databases

    PaxDbiP08308.
    PRIDEiP08308.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG08557; AAG08557; PA5172.
    GeneIDi881792.
    KEGGipae:PA5172.
    PATRICi19845187. VBIPseAer58763_5420.

    Organism-specific databases

    PseudoCAPiPA5172.

    Phylogenomic databases

    eggNOGiENOG4105DBV. Bacteria.
    COG0078. LUCA.
    HOGENOMiHOG000022686.
    InParanoidiP08308.
    KOiK00611.
    OMAiMGMEIRL.
    PhylomeDBiP08308.

    Enzyme and pathway databases

    UniPathwayiUPA00254; UER00365.
    SABIO-RKP08308.

    Miscellaneous databases

    EvolutionaryTraceiP08308.

    Family and domain databases

    Gene3Di3.40.50.1370. 2 hits.
    HAMAPiMF_01109. OTCase. 1 hit.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR002292. Orn/put_carbamltrans.
    IPR024904. OTCase_ArgI.
    [Graphical view]
    PfamiPF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view]
    PRINTSiPR00100. AOTCASE.
    PR00102. OTCASE.
    SUPFAMiSSF53671. SSF53671. 1 hit.
    TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
    PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiOTCC_PSEAE
    AccessioniPrimary (citable) accession number: P08308
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Proceeds by an ordered sequential mechanism with CP identified as the initial reactant.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.