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Protein

N-acetylornithine carbamoyltransferase

Gene

argF'

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.

Catalytic activityi

Carbamoyl phosphate + N(2)-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline.

Pathwayi: L-arginine biosynthesis

This protein is involved in the pathway L-arginine biosynthesis, which is part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121Carbamoyl phosphate
Binding sitei148 – 1481Carbamoyl phosphate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12073.
XCAM190485:GIXZ-2247-MONOMER.
BRENDAi2.1.3.9. 6708.
UniPathwayiUPA00068.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylornithine carbamoyltransferase (EC:2.1.3.9)
Short name:
AOTCase
Gene namesi
Name:argF'
Ordered Locus Names:XCC2249
OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Taxonomic identifieri190485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
Proteomesi
  • UP000001010 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339N-acetylornithine carbamoyltransferasePRO_0000113268Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

STRINGi190485.XCC2249.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Helixi14 – 2916Combined sources
Turni35 – 384Combined sources
Beta strandi40 – 478Combined sources
Helixi50 – 6213Combined sources
Beta strandi66 – 705Combined sources
Helixi72 – 754Combined sources
Beta strandi82 – 843Combined sources
Helixi95 – 10511Combined sources
Beta strandi107 – 1126Combined sources
Helixi120 – 1234Combined sources
Turni124 – 1263Combined sources
Helixi127 – 1359Combined sources
Beta strandi140 – 1467Combined sources
Helixi149 – 16315Combined sources
Beta strandi172 – 1776Combined sources
Helixi187 – 19812Combined sources
Beta strandi202 – 2065Combined sources
Helixi210 – 2123Combined sources
Helixi216 – 22914Combined sources
Beta strandi232 – 2365Combined sources
Helixi239 – 2435Combined sources
Beta strandi247 – 2526Combined sources
Helixi257 – 2593Combined sources
Helixi266 – 2705Combined sources
Helixi271 – 2766Combined sources
Helixi280 – 2845Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi290 – 2923Combined sources
Turni299 – 3013Combined sources
Helixi305 – 3084Combined sources
Helixi315 – 33319Combined sources

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei28 – 281Important for structural integrityBy similarity
Sitei161 – 1611Important for structural integrityBy similarity

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KZCX-ray2.20A1-339[»]
3KZKX-ray1.90A1-339[»]
3KZMX-ray1.95A1-339[»]
3KZNX-ray1.80A1-339[»]
3KZOX-ray1.90A1-339[»]
3L02X-ray2.30A1-339[»]
3L04X-ray2.50A1-339[»]
3L05X-ray2.80A1-339[»]
3L06X-ray2.81A1-339[»]
3M4JX-ray2.20A1-339[»]
3M4NX-ray1.90A1-339[»]
3M5CX-ray1.85A1-339[»]
3M5DX-ray2.20A1-339[»]
ProteinModelPortaliQ8P8J2.
SMRiQ8P8J2. Positions 3-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8P8J2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 535Carbamoyl phosphate binding
Regioni293 – 2964N-acetylornithine binding

Sequence similaritiesi

Belongs to the ATCase/OTCase family.Curated

Phylogenomic databases

eggNOGiENOG4105DBV. Bacteria.
COG0078. LUCA.
HOGENOMiHOG000022686.
KOiK09065.
OMAiEHALFAN.
OrthoDBiEOG6G4VSH.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8P8J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKHFLNTQ DWSRAELDAL LTQAALFKRN KLGSELKGKS IALVFFNPSM
60 70 80 90 100
RTRTSFELGA FQLGGHAVVL QPGKDAWPIE FNLGTVMDGD TEEHIAEVAR
110 120 130 140 150
VLGRYVDLIG VRAFPKFVDW SKDREDQVLK SFAKYSPVPV INMETITHPC
160 170 180 190 200
QELAHALALQ EHFGTPDLRG KKYVLTWTYH PKPLNTAVAN SALTIATRMG
210 220 230 240 250
MDVTLLCPTP DYILDERYMD WAAQNVAESG GSLQVSHDID SAYAGADVVY
260 270 280 290 300
AKSWGALPFF GNWEPEKPIR DQYQHFIVDE RKMALTNNGV FSHCLPLRRN
310 320 330
VKATDAVMDS PNCIAIDEAE NRLHVQKAIM AALVGQSRP
Length:339
Mass (Da):37,873
Last modified:October 1, 2002 - v1
Checksum:i8FEFBA16773A00D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008922 Genomic DNA. Translation: AAM41528.1.
RefSeqiNP_637604.1. NC_003902.1.
WP_011037393.1. NC_003902.1.

Genome annotation databases

EnsemblBacteriaiAAM41528; AAM41528; XCC2249.
GeneIDi998828.
KEGGixcc:XCC2249.
PATRICi24075403. VBIXanCam115730_2399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008922 Genomic DNA. Translation: AAM41528.1.
RefSeqiNP_637604.1. NC_003902.1.
WP_011037393.1. NC_003902.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KZCX-ray2.20A1-339[»]
3KZKX-ray1.90A1-339[»]
3KZMX-ray1.95A1-339[»]
3KZNX-ray1.80A1-339[»]
3KZOX-ray1.90A1-339[»]
3L02X-ray2.30A1-339[»]
3L04X-ray2.50A1-339[»]
3L05X-ray2.80A1-339[»]
3L06X-ray2.81A1-339[»]
3M4JX-ray2.20A1-339[»]
3M4NX-ray1.90A1-339[»]
3M5CX-ray1.85A1-339[»]
3M5DX-ray2.20A1-339[»]
ProteinModelPortaliQ8P8J2.
SMRiQ8P8J2. Positions 3-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190485.XCC2249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM41528; AAM41528; XCC2249.
GeneIDi998828.
KEGGixcc:XCC2249.
PATRICi24075403. VBIXanCam115730_2399.

Phylogenomic databases

eggNOGiENOG4105DBV. Bacteria.
COG0078. LUCA.
HOGENOMiHOG000022686.
KOiK09065.
OMAiEHALFAN.
OrthoDBiEOG6G4VSH.

Enzyme and pathway databases

UniPathwayiUPA00068.
BioCyciMetaCyc:MONOMER-12073.
XCAM190485:GIXZ-2247-MONOMER.
BRENDAi2.1.3.9. 6708.

Miscellaneous databases

EvolutionaryTraceiQ8P8J2.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
    da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
    , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
    Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25.
  2. "Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria."
    Shi D., Morizono H., Yu X., Roth L., Caldovic L., Allewell N.M., Malamy M.H., Tuchman M.
    J. Biol. Chem. 280:14366-14369(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiAOTC_XANCP
AccessioniPrimary (citable) accession number: Q8P8J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: October 1, 2002
Last modified: February 17, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.