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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

Involved in the catabolism of arginine. Catalyzes the phosphorolysis of citrulline, the reverse reaction of the biosynthetic one, yielding ornithine and carbamoyl phosphate which serve to generate ATP from ADP (PubMed:4962140, PubMed:2118516). This catabolic OTCase does not carry out the biosynthetic reaction because of a poor affinity and a marked cooperativity for carbamoyl phosphate (PubMed:2118516).3 Publications2 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by 2-aminopentanoic acid (norvaline). Activated by phosphate and nucleoside monophosphates such as AMP, GMP, CMP, UMP. Allosterically inhibited by the polyamines such as spermidine and putrescine.1 Publication

pH dependencei

Optimum pH is 7.3.1 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.3 Publications
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 sitei84Carbamoyl phosphateUniRule annotation1
Binding sitei108Carbamoyl phosphateUniRule annotation1
Binding sitei168OrnithineUniRule annotation1
Binding sitei232OrnithineUniRule annotation1
Binding sitei321Carbamoyl phosphateUniRule annotation1

GO - Molecular functioni

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

GO - Biological processi

  • arginine catabolic process to ornithine Source: UniProtKB-UniPathway
  • arginine deiminase pathway Source: PseudoCAP

Keywordsi

Molecular functionTransferase
Biological processArginine metabolism

Enzyme and pathway databases

SABIO-RKP08308.
UniPathwayiUPA00254; UER00365.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine carbamoyltransferase, catabolic1 Publication (EC:2.1.3.3UniRule annotation)
Short name:
OTCase1 Publication
Gene namesi
Name:arcB1 Publication
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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are blocked in the arginine deiminase pathway.1 Publication

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. This mutant is blocked in the active R (relaxed) state. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001129862 – 336Ornithine carbamoyltransferase, catabolicAdd BLAST335

Proteomic databases

PaxDbiP08308.
PRIDEiP08308.

Expressioni

Inductioni

During limiting aeration and in the presence of arginine.1 Publication1 Publication

Interactioni

Subunit structurei

Nonameric or dodecamer (tetramer of trimers).4 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

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
Regioni57 – 60Carbamoyl phosphate bindingUniRule annotation4
Regioni135 – 138Carbamoyl phosphate bindingUniRule annotation4
Regioni236 – 237Ornithine bindingUniRule annotation2
Regioni274 – 275Carbamoyl phosphate bindingUniRule annotation2

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.
InterProiView protein in InterPro
IPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
IPR024904. OTCase_ArgI.
PfamiView protein in Pfam
PF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
PRINTSiPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
PROSITEiView protein in PROSITE
PS00097. CARBAMOYLTRANSFERASE. 1 hit.

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.
InterProiView protein in InterPro
IPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
IPR024904. OTCase_ArgI.
PfamiView protein in Pfam
PF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
PRINTSiPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
PROSITEiView protein in PROSITE
PS00097. CARBAMOYLTRANSFERASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiOTCC_PSEAE
AccessioniPrimary (citable) accession number: P08308
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: March 15, 2017
This is version 143 of the entry and version 3 of the sequence. See 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.