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Q48296 (OTCC_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine carbamoyltransferase, catabolic

Short name=cOTCase
EC=2.1.3.3
Gene names
Name:arcB
Synonyms:argB
Ordered Locus Names:VNG_6315G
Encoded onPlasmid pNRC200 Ref.3
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. HAMAP-Rule MF_01109

Enzyme regulation

Arginine lead to a slight activation. Inhibited by all nucleotide phosphates. Ref.1

Pathway

Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2. HAMAP-Rule MF_01109

Subunit structure

Homohexamer. Ref.1

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_01109.

Miscellaneous

Not stable below 1 M KCl (Ref.1).

Sequence similarities

Belongs to the ATCase/OTCase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.4 mM for carbamoyl phosphate Ref.1

KM=8 mM for L-ornithine

pH dependence:

Optimum pH is 8.8. At the physiological pH of 7, activity is only about 30%.

Ontologies

Keywords
   Biological processArginine metabolism
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Direct protein sequencing
Plasmid
Reference proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process to ornithine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

arginine deiminase pathway

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: InterPro

ornithine carbamoyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Ornithine carbamoyltransferase, catabolic HAMAP-Rule MF_01109
PRO_0000113063

Regions

Region49 – 535Carbamoyl phosphate binding By similarity
Region127 – 1304Carbamoyl phosphate binding By similarity
Region217 – 2182Ornithine binding By similarity
Region252 – 2554Carbamoyl phosphate binding By similarity

Sites

Binding site51Carbamoyl phosphate By similarity
Binding site651Carbamoyl phosphate By similarity
Binding site761Carbamoyl phosphate By similarity
Binding site1001Carbamoyl phosphate By similarity
Binding site1551Ornithine By similarity
Binding site2131Ornithine By similarity
Binding site2631Carbamoyl phosphate By similarity
Binding site2811Carbamoyl phosphate By similarity
Site261Important for structural integrity By similarity
Site1401Important for structural integrity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48296 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BFF6E002AC0289A2

FASTA29532,676
        10         20         30         40         50         60 
MEHLVDINDV ESEEIEQLLD LAASMKENPG EFSGVMDNKS LVMLFAKPST RTRLSFETGM 

        70         80         90        100        110        120 
TQLGGHGIFF EMGSSQLSRG EPISDVSQVM SRYEDAIMAR LFEHDEMMEL AENADVPVVN 

       130        140        150        160        170        180 
GLTDFLHPCQ ALTDMFTMQE KDRLDTLAFV GDGNNVAHSL MQASAKMGVD CRIATPEGME 

       190        200        210        220        230        240 
PDEEIQDRVS DANVTVTNDP YEAVDGATAV YGDVFVSMGE EEQREEKLAE FDGFQIDQDL 

       250        260        270        280        290 
MDAARDDAIF MHCLPAHRGE EVTAEVADGP QSVIFDQAEN RMHVQKAIVH TLVNQ 

« Hide

References

« Hide 'large scale' references
[1]"Catabolic ornithine transcarbamylase of Halobacterium halobium (salinarium): purification, characterization, sequence determination, and evolution."
Ruepp A., Mueller H., Lottspeich F., Soppa J.
J. Bacteriol. 177:1129-1136(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS A COTCASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
Strain: R1 / S9 / L33.
[2]"Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster."
Ruepp A., Soppa J.
J. Bacteriol. 178:4942-4947(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: R1 / S9 / L33.
[3]"Genome sequence of Halobacterium species NRC-1."
Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. expand/collapse author list , Cruz R., Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.
Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700922 / JCM 11081 / NRC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81712 Genomic DNA. Translation: CAA57356.1.
X80931 Genomic DNA. Translation: CAA56906.1.
AE004438 Genomic DNA. Translation: AAG20946.1.
PIRS49261.
RefSeqNP_395811.1. NC_002608.1.

3D structure databases

ProteinModelPortalQ48296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64091.VNG6315G.

Proteomic databases

PaxDbQ48296.
PRIDEQ48296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG20946; AAG20946; VNG_6315G.
GeneID1449194.
KEGGhal:VNG6315G.

Phylogenomic databases

eggNOGCOG0078.
KOK00611.
OMATAKMMKI.
PhylomeDBQ48296.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-662.
UniPathwayUPA00254; UER00365.

Family and domain databases

Gene3D3.40.50.1370. 2 hits.
HAMAPMF_01109. OTCase.
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
IPR024904. Orn_carbamltrans.
[Graphical view]
PfamPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMSSF53671. SSF53671. 1 hit.
TIGRFAMsTIGR00658. orni_carb_tr. 1 hit.
PROSITEPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOTCC_HALSA
AccessionPrimary (citable) accession number: Q48296
Secondary accession number(s): Q59454, Q9HHN0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways