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Protein

Ornithine carbamoyltransferase chain I

Gene

argI

Organism
Escherichia coli (strain K12)
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, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.2 Publications

Catalytic activityi

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

Enzyme regulationi

Reversely inhibited by N-(N-Sulfodiaminophosphinyl)-L-ornithine. Zinc is an allosteric regulator of the substrate-bound enzyme and a competitive inhibitor of the free euzyme.4 Publications

Kineticsi

  1. KM=50 µM for carbamoyl phosphate3 Publications
  2. KM=0.18 mM for L-ornithine3 Publications
  3. KM=0.32 mM for L-ornithine3 Publications
  1. Vmax=0.29 µmol/min/µg enzyme3 Publications

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Ornithine carbamoyltransferase chain I (argI), Ornithine carbamoyltransferase chain F (argF)
  2. Argininosuccinate synthase (argG)
  3. Argininosuccinate lyase (argH)
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 L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Carbamoyl phosphateBy similarity
Binding sitei72 – 721Carbamoyl phosphateBy similarity
Binding sitei83 – 831Carbamoyl phosphate
Binding sitei107 – 1071Carbamoyl phosphate
Binding sitei168 – 1681Ornithine
Binding sitei232 – 2321Ornithine
Metal bindingi274 – 2741Zinc
Binding sitei302 – 3021Carbamoyl phosphateBy similarity
Binding sitei320 – 3201Carbamoyl phosphate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:CHAINI-MONOMER.
ECOL316407:JW4211-MONOMER.
MetaCyc:CHAINI-MONOMER.
BRENDAi2.1.3.3. 2026.
SABIO-RKP04391.
UniPathwayiUPA00068; UER00112.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine carbamoyltransferase chain I (EC:2.1.3.3)
Alternative name(s):
OTCase-1
Gene namesi
Name:argI
Ordered Locus Names:b4254, JW4211
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10069. argI.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561S → H: Much less active than the wild-type. 1 Publication
Mutagenesisi58 – 581R → G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate. 2 Publications
Mutagenesisi87 – 871K → Q: Much less active than the wild-type. 1 Publication
Mutagenesisi274 – 2741C → A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization. 1 Publication
Mutagenesisi320 – 3201R → A: Much less active than the wild-type. 1 Publication
Mutagenesisi326 – 3261A → G: Activity greater than the wild-type and Km for ornithwinas increases about twofold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 334333Ornithine carbamoyltransferase chain IPRO_0000112918Add
BLAST

Proteomic databases

EPDiP04391.
PaxDbiP04391.
PRIDEiP04391.

2D gel databases

SWISS-2DPAGEP04391.

Interactioni

Subunit structurei

In E.coli strain K12, trimer of identical or non-identical chains are composed of ArgI (I) and/or ArgF (F). The trimer has the following composition: FFI, FFF, FII, III. E.coli strains B and W, which are known to contain only ArgI, produce only a trimer of identical chains (III).5 Publications

Protein-protein interaction databases

BioGridi4262723. 6 interactions.
DIPiDIP-9143N.
IntActiP04391. 7 interactions.
STRINGi511145.b4254.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Helixi12 – 143Combined sources
Helixi17 – 3519Combined sources
Beta strandi47 – 548Combined sources
Helixi58 – 6912Combined sources
Beta strandi73 – 775Combined sources
Beta strandi79 – 824Combined sources
Turni85 – 873Combined sources
Helixi90 – 978Combined sources
Turni98 – 1003Combined sources
Beta strandi102 – 1076Combined sources
Helixi111 – 12111Combined sources
Beta strandi125 – 1284Combined sources
Helixi135 – 14814Combined sources
Helixi154 – 1563Combined sources
Beta strandi158 – 1636Combined sources
Helixi168 – 18013Combined sources
Beta strandi183 – 1875Combined sources
Helixi190 – 1923Combined sources
Helixi196 – 20813Combined sources
Beta strandi212 – 2176Combined sources
Helixi219 – 2235Combined sources
Beta strandi227 – 2315Combined sources
Helixi243 – 2519Combined sources
Helixi252 – 2543Combined sources
Helixi258 – 2625Combined sources
Turni263 – 2653Combined sources
Beta strandi270 – 2734Combined sources
Helixi284 – 2929Combined sources
Beta strandi297 – 3026Combined sources
Helixi303 – 3064Combined sources
Beta strandi308 – 3114Combined sources
Helixi313 – 33220Combined sources

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei31 – 311Important for structural integrity
Sitei147 – 1471Important for structural integrity

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKMX-ray2.80A/B/C2-334[»]
1DUVX-ray1.70G/H/I2-334[»]
2OTCX-ray2.80A/B/C/D/E/F/G/H/I2-334[»]
ProteinModelPortaliP04391.
SMRiP04391. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04391.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 605Carbamoyl phosphate binding
Regioni134 – 1374Carbamoyl phosphate binding
Regioni236 – 2372Ornithine binding
Regioni273 – 2764Carbamoyl phosphate binding

Sequence similaritiesi

Belongs to the ATCase/OTCase family.Curated

Phylogenomic databases

eggNOGiENOG4105DBV. Bacteria.
COG0078. LUCA.
HOGENOMiHOG000022686.
InParanoidiP04391.
KOiK00611.
OMAiCWPEAEL.
OrthoDBiEOG690MGV.
PhylomeDBiP04391.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_01109. OTCase.
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.

P04391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGFYHKHFL KLLDFTPAEL NSLLQLAAKL KADKKSGKEE AKLTGKNIAL
60 70 80 90 100
IFEKDSTRTR CSFEVAAYDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM
110 120 130 140 150
YDGIQYRGYG QEIVETLAEY ASVPVWNGLT NEFHPTQLLA DLLTMQEHLP
160 170 180 190 200
GKAFNEMTLV YAGDARNNMG NSMLEAAALT GLDLRLVAPQ ACWPEAALVT
210 220 230 240 250
ECRALAQQNG GNITLTEDVA KGVEGADFIY TDVWVSMGEA KEKWAERIAL
260 270 280 290 300
LREYQVNSKM MQLTGNPEVK FLHCLPAFHD DQTTLGKKMA EEFGLHGGME
310 320 330
VTDEVFESAA SIVFDQAENR MHTIKAVMVA TLSK
Length:334
Mass (Da):36,907
Last modified:January 23, 2007 - v3
Checksum:i75D67EE69C229E5C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121L → G AA sequence (PubMed:9298646).Curated
Sequence conflicti119 – 1191E → Q in CAA25037 (PubMed:6369246).Curated
Sequence conflicti121 – 1211A → R in CAA25037 (PubMed:6369246).Curated
Sequence conflicti139 – 1424LADL → IEYK in CAA25037 (PubMed:6369246).Curated
Sequence conflicti242 – 2421E → Q in CAA25037 (PubMed:6369246).Curated
Sequence conflicti252 – 2521R → A in CAA25037 (PubMed:6369246).Curated
Sequence conflicti315 – 3151D → G in CAA25037 (PubMed:6369246).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02842 Genomic DNA. Translation: AAA23483.1.
X00210 Genomic DNA. Translation: CAA25037.1.
U14003 Genomic DNA. Translation: AAA97150.1.
U00096 Genomic DNA. Translation: AAC77211.1.
AP009048 Genomic DNA. Translation: BAE78251.1.
PIRiA31314. OWECI.
RefSeqiNP_418675.1. NC_000913.3.
WP_000012931.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77211; AAC77211; b4254.
BAE78251; BAE78251; BAE78251.
GeneIDi948774.
KEGGiecj:JW4211.
eco:b4254.
PATRICi32124079. VBIEscCol129921_4384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02842 Genomic DNA. Translation: AAA23483.1.
X00210 Genomic DNA. Translation: CAA25037.1.
U14003 Genomic DNA. Translation: AAA97150.1.
U00096 Genomic DNA. Translation: AAC77211.1.
AP009048 Genomic DNA. Translation: BAE78251.1.
PIRiA31314. OWECI.
RefSeqiNP_418675.1. NC_000913.3.
WP_000012931.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKMX-ray2.80A/B/C2-334[»]
1DUVX-ray1.70G/H/I2-334[»]
2OTCX-ray2.80A/B/C/D/E/F/G/H/I2-334[»]
ProteinModelPortaliP04391.
SMRiP04391. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262723. 6 interactions.
DIPiDIP-9143N.
IntActiP04391. 7 interactions.
STRINGi511145.b4254.

2D gel databases

SWISS-2DPAGEP04391.

Proteomic databases

EPDiP04391.
PaxDbiP04391.
PRIDEiP04391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77211; AAC77211; b4254.
BAE78251; BAE78251; BAE78251.
GeneIDi948774.
KEGGiecj:JW4211.
eco:b4254.
PATRICi32124079. VBIEscCol129921_4384.

Organism-specific databases

EchoBASEiEB0067.
EcoGeneiEG10069. argI.

Phylogenomic databases

eggNOGiENOG4105DBV. Bacteria.
COG0078. LUCA.
HOGENOMiHOG000022686.
InParanoidiP04391.
KOiK00611.
OMAiCWPEAEL.
OrthoDBiEOG690MGV.
PhylomeDBiP04391.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00112.
BioCyciEcoCyc:CHAINI-MONOMER.
ECOL316407:JW4211-MONOMER.
MetaCyc:CHAINI-MONOMER.
BRENDAi2.1.3.3. 2026.
SABIO-RKP04391.

Miscellaneous databases

EvolutionaryTraceiP04391.
PROiP04391.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_01109. OTCase.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis."
    Kuo L.C., Miller A.W., Lee S., Kozuma C.
    Biochemistry 27:8823-8832(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ARG-58, BIOPHYSICOCHEMICAL PROPERTIES.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  7. "The dual genetic control of ornithine carbamolytransferase in Escherichia coli. A case of bacterial hybrid enzymes."
    Legrain C., Halleux P., Stalon V., Glansdorff N.
    Eur. J. Biochem. 27:93-102(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary significance and the isolation of lambdaargF and lambdaargI transducing bacteriophages."
    Legrain C., Stalon V., Glansdorff N.
    J. Bacteriol. 128:35-38(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  9. "Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylase."
    Kuo L.C., Lipscomb W.N., Kantrowitz E.R.
    Proc. Natl. Acad. Sci. U.S.A. 79:2250-2254(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  10. "X-ray diffraction analysis on single crystals of recombinant Escherichia coli ornithine transcarbamoylase."
    Kuo L.C., Seaton B.A.
    J. Biol. Chem. 264:16246-16248(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-58.
  11. "Zn2+ regulation of ornithine transcarbamoylase. I. Mechanism of action."
    Lee S., Shen W.H., Miller A.W., Kuo L.C.
    J. Mol. Biol. 211:255-269(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  12. "Zn2+ regulation of ornithine transcarbamoylase. II. Metal binding site."
    Kuo L.C., Caron C., Lee S., Herzberg W.
    J. Mol. Biol. 211:271-280(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-274, ENZYME REGULATION.
  13. "Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase."
    Murata L.B., Schachman H.K.
    Protein Sci. 5:709-718(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-56; LYS-87; ARG-320 AND ALA-326, BIOPHYSICOCHEMICAL PROPERTIES.
  14. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  15. "Crystal structure at 2.8-A resolution of anabolic ornithine transcarbamylase from Escherichia coli."
    Jin L., Seaton B.A., Head J.F.
    Nat. Struct. Biol. 4:622-625(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.
  16. "Substrate-induced conformational change in a trimeric ornithine transcarbamoylase."
    Ha Y., McCann M.T., Tuchman M., Allewell N.M.
    Proc. Natl. Acad. Sci. U.S.A. 94:9550-9555(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
  17. "Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism."
    Langley D.B., Templeton M.D., Fields B.A., Mitchell R.E., Collyer C.A.
    J. Biol. Chem. 275:20012-20019(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-333 IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiOTC1_ECOLI
AccessioniPrimary (citable) accession number: P04391
Secondary accession number(s): Q2M655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.