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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)DescriptionActionsGraphical viewLength
Binding sitei10Carbamoyl phosphateBy similarity1
Binding sitei72Carbamoyl phosphateBy similarity1
Binding sitei83Carbamoyl phosphate1
Binding sitei107Carbamoyl phosphate1
Binding sitei168Ornithine1
Binding sitei232Ornithine1
Metal bindingi274Zinc1
Binding sitei302Carbamoyl phosphateBy similarity1
Binding sitei320Carbamoyl phosphate1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi56S → H: Much less active than the wild-type. 1 Publication1
Mutagenesisi58R → G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate. 2 Publications1
Mutagenesisi87K → Q: Much less active than the wild-type. 1 Publication1
Mutagenesisi274C → A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization. 1 Publication1
Mutagenesisi320R → A: Much less active than the wild-type. 1 Publication1
Mutagenesisi326A → G: Activity greater than the wild-type and Km for ornithwinas increases about twofold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001129182 – 334Ornithine carbamoyltransferase chain IAdd BLAST333

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 interactors.
DIPiDIP-9143N.
IntActiP04391. 7 interactors.
STRINGi511145.b4254.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Helixi12 – 14Combined sources3
Helixi17 – 35Combined sources19
Beta strandi47 – 54Combined sources8
Helixi58 – 69Combined sources12
Beta strandi73 – 77Combined sources5
Beta strandi79 – 82Combined sources4
Turni85 – 87Combined sources3
Helixi90 – 97Combined sources8
Turni98 – 100Combined sources3
Beta strandi102 – 107Combined sources6
Helixi111 – 121Combined sources11
Beta strandi125 – 128Combined sources4
Helixi135 – 148Combined sources14
Helixi154 – 156Combined sources3
Beta strandi158 – 163Combined sources6
Helixi168 – 180Combined sources13
Beta strandi183 – 187Combined sources5
Helixi190 – 192Combined sources3
Helixi196 – 208Combined sources13
Beta strandi212 – 217Combined sources6
Helixi219 – 223Combined sources5
Beta strandi227 – 231Combined sources5
Helixi243 – 251Combined sources9
Helixi252 – 254Combined sources3
Helixi258 – 262Combined sources5
Turni263 – 265Combined sources3
Beta strandi270 – 273Combined sources4
Helixi284 – 292Combined sources9
Beta strandi297 – 302Combined sources6
Helixi303 – 306Combined sources4
Beta strandi308 – 311Combined sources4
Helixi313 – 332Combined sources20

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei31Important for structural integrity1
Sitei147Important for structural integrity1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04391.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni56 – 60Carbamoyl phosphate binding5
Regioni134 – 137Carbamoyl phosphate binding4
Regioni236 – 237Ornithine binding2
Regioni273 – 276Carbamoyl phosphate binding4

Sequence similaritiesi

Belongs to the ATCase/OTCase family.Curated

Phylogenomic databases

eggNOGiENOG4105DBV. Bacteria.
COG0078. LUCA.
HOGENOMiHOG000022686.
InParanoidiP04391.
KOiK00611.
OMAiSACWPEA.
PhylomeDBiP04391.

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti12L → G AA sequence (PubMed:9298646).Curated1
Sequence conflicti119E → Q in CAA25037 (PubMed:6369246).Curated1
Sequence conflicti121A → R in CAA25037 (PubMed:6369246).Curated1
Sequence conflicti139 – 142LADL → IEYK in CAA25037 (PubMed:6369246).Curated4
Sequence conflicti242E → Q in CAA25037 (PubMed:6369246).Curated1
Sequence conflicti252R → A in CAA25037 (PubMed:6369246).Curated1
Sequence conflicti315D → G in CAA25037 (PubMed:6369246).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262723. 6 interactors.
DIPiDIP-9143N.
IntActiP04391. 7 interactors.
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.
OMAiSACWPEA.
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. 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 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: November 2, 2016
This is version 168 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.