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Entry version 194 (07 Oct 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Ornithine carbamoyltransferase subunit I

Gene

argI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Reversely inhibited by N-(N-Sulfodiaminophosphinyl)-L-ornithine (PubMed:10747936). Zinc is an allosteric regulator of the substrate-bound enzyme and a competitive inhibitor of the free enzyme (PubMed:7048313, PubMed:2105398, PubMed:2405164).4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 14000 min(-1) for L-ornithine. Kcat is 13000 min(-1) for carbamoyl phosphate.1 Publication
  1. KM=10 µM for carbamoyl phosphate1 Publication
  2. KM=50 µM for carbamoyl phosphate1 Publication
  3. KM=0.18 mM for L-ornithine1 Publication
  4. KM=0.32 mM for L-ornithine1 Publication
  5. KM=5 mM for L-ornithine1 Publication
  1. Vmax=0.29 µmol/min/µg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.Curated
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Ornithine carbamoyltransferase subunit F (argF), Ornithine carbamoyltransferase (argF), Ornithine carbamoyltransferase subunit I (argI)
  2. Argininosuccinate synthase (argG), Argininosuccinate synthase (argG)
  3. Argininosuccinate lyase (argH), 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei83Carbamoyl phosphateCombined sources2 Publications1
Binding sitei107Carbamoyl phosphateCombined sources2 Publications1
Binding sitei168OrnithineCombined sources2 Publications1
Binding sitei232OrnithineCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi274Zinc1 Publication1
Binding sitei320Carbamoyl phosphateCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Transferase
Biological processAmino-acid biosynthesis, Arginine biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:CHAINI-MONOMER
MetaCyc:CHAINI-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.3.3, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P04391

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00068;UER00112

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ornithine carbamoyltransferase subunit I1 Publication (EC:2.1.3.31 Publication)
Short name:
OTCase-11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:argI1 Publication
Ordered Locus Names:b4254, JW4211
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02965, Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001129182 – 334Ornithine carbamoyltransferase subunit IAdd BLAST333

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P04391

PRoteomics IDEntifications database

More...
PRIDEi
P04391

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P04391

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

In E.coli strain K12, trimer of identical or non-identical chains are composed of ArgI (I) and/or ArgF (F) (PubMed:6369246, PubMed:4558857, PubMed:789338). The trimer has the following composition: FFI, FFF, FII, III (PubMed:6369246, PubMed:4558857, PubMed:789338). E.coli strains B and W, which are known to contain only ArgI, produce only a trimer of identical chains (III).

6 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262723, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-5624, Ornithine transcarbamoylase complex, argIII variant
CPX-5625, Ornithine transcarbamoylase complex, argFII variant
CPX-5626, Ornithine transcarbamoylase complex, argFFI variant

Database of interacting proteins

More...
DIPi
DIP-9143N

Protein interaction database and analysis system

More...
IntActi
P04391, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b4254

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04391

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04391

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni56 – 59Carbamoyl phosphate bindingCombined sources2 Publications4
Regioni134 – 137Carbamoyl phosphate bindingCombined sources2 Publications4
Regioni236 – 237Ornithine bindingCombined sources2 Publications2
Regioni274 – 275Carbamoyl phosphate bindingCombined sources2 Publications2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0078, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_043846_3_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P04391

KEGG Orthology (KO)

More...
KOi
K00611

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P04391

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1370, 2 hits

HAMAP database of protein families

More...
HAMAPi
MF_01109, OTCase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006132, Asp/Orn_carbamoyltranf_P-bd
IPR006130, Asp/Orn_carbamoylTrfase
IPR036901, Asp/Orn_carbamoylTrfase_sf
IPR006131, Asp_carbamoyltransf_Asp/Orn-bd
IPR002292, Orn/put_carbamltrans
IPR024904, OTCase_ArgI

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00185, OTCace, 1 hit
PF02729, OTCace_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00100, AOTCASE
PR00102, OTCASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53671, SSF53671, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00658, orni_carb_tr, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00097, CARBAMOYLTRANSFERASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i75D67EE69C229E5C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X00210 Genomic DNA Translation: CAA25037.1
J02842 Genomic DNA Translation: AAA23483.1
U14003 Genomic DNA Translation: AAA97150.1
U00096 Genomic DNA Translation: AAC77211.1
AP009048 Genomic DNA Translation: BAE78251.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A31314, OWECI

NCBI Reference Sequences

More...
RefSeqi
NP_418675.1, NC_000913.3
WP_000012931.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77211; AAC77211; b4254
BAE78251; BAE78251; BAE78251

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948774

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4211
eco:b4254

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2450

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00210 Genomic DNA Translation: CAA25037.1
J02842 Genomic DNA Translation: AAA23483.1
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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiP04391
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262723, 6 interactors
ComplexPortaliCPX-5624, Ornithine transcarbamoylase complex, argIII variant
CPX-5625, Ornithine transcarbamoylase complex, argFII variant
CPX-5626, Ornithine transcarbamoylase complex, argFFI variant
DIPiDIP-9143N
IntActiP04391, 7 interactors
STRINGi511145.b4254

Chemistry databases

DrugBankiDB02965, Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine

2D gel databases

SWISS-2DPAGEiP04391

Proteomic databases

PaxDbiP04391
PRIDEiP04391

Genome annotation databases

EnsemblBacteriaiAAC77211; AAC77211; b4254
BAE78251; BAE78251; BAE78251
GeneIDi948774
KEGGiecj:JW4211
eco:b4254
PATRICifig|1411691.4.peg.2450

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0067

Phylogenomic databases

eggNOGiCOG0078, Bacteria
HOGENOMiCLU_043846_3_1_6
InParanoidiP04391
KOiK00611
PhylomeDBiP04391

Enzyme and pathway databases

UniPathwayiUPA00068;UER00112
BioCyciEcoCyc:CHAINI-MONOMER
MetaCyc:CHAINI-MONOMER
BRENDAi2.1.3.3, 2026
SABIO-RKiP04391

Miscellaneous databases

EvolutionaryTraceiP04391

Protein Ontology

More...
PROi
PR:P04391

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
IPR036901, Asp/Orn_carbamoylTrfase_sf
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOTC1_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04391
Secondary accession number(s): Q2M655
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: October 7, 2020
This is version 194 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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