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E4WH16 (E4WH16_RHOE1) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase large chain HAMAP-Rule MF_01210

EC=6.3.5.5 HAMAP-Rule MF_01210
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain HAMAP-Rule MF_01210
Gene names
Name:carB HAMAP-Rule MF_01210 EMBL CBH48221.1
Ordered Locus Names:REQ_21680 EMBL CBH48221.1
OrganismRhodococcus equi (strain 103S) (Corynebacterium equi) [Complete proteome] [HAMAP] EMBL CBH48221.1
Taxonomic identifier685727 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length1115 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. SAAS SAAS005483 HAMAP-Rule MF_01210

Cofactor

Binds 4 magnesium or manganese ions per subunit By similarity. HAMAP-Rule MF_01210 SAAS SAAS005483

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP-Rule MF_01210 SAAS SAAS005483

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP-Rule MF_01210 SAAS SAAS005483

Subunit structure

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate By similarity. HAMAP-Rule MF_01210 SAAS SAAS005483

Sequence similarities

Belongs to the CarB family. HAMAP-Rule MF_01210

Contains 2 ATP-grasp domains. HAMAP-Rule MF_01210

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain138 – 333196ATP-grasp 1 By similarity HAMAP-Rule MF_01210
Domain694 – 885192ATP-grasp 2 By similarity HAMAP-Rule MF_01210
Nucleotide binding164 – 22158ATP By similarity HAMAP-Rule MF_01210
Nucleotide binding720 – 77758ATP By similarity HAMAP-Rule MF_01210
Region1 – 407407Carboxyphosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region408 – 564157Oligomerization domain By similarity HAMAP-Rule MF_01210
Region565 – 966402Carbamoyl phosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region967 – 1115149Allosteric domain By similarity HAMAP-Rule MF_01210

Sites

Metal binding2901Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding3041Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding3041Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding3061Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding8441Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8561Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8561Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210
Metal binding8581Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210

Sequences

Sequence LengthMass (Da)Tools
E4WH16 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 85E7D80ECA0C1880

FASTA1,115119,924
        10         20         30         40         50         60 
MPRRTDLEHI LVIGSGPIVI GQACEFDYSG TQACRVLREE GLRVSLVNSN PATIMTDPEF 

        70         80         90        100        110        120 
ADSTYVEPIT AEFVEKVIAR EAANGNKIDA VLATLGGQTA LNTAVALHEQ GILEKYDVEL 

       130        140        150        160        170        180 
IGADFDAIQR GEDRQKFKDI VEKCGGESAR SRVCYTMEEV KATVAELGYP VVVRPSFTMG 

       190        200        210        220        230        240 
GLGSGMAYDE VDLERIAGGG LAASPTANVL IEESILGWKE YELELMRDGR DNVVIVCSIE 

       250        260        270        280        290        300 
NVDPVGVHTG DSVTVAPAMT LTDREYQAMR DLSIAILREV GVDTGGCNIQ FAMDPKDGRL 

       310        320        330        340        350        360 
VVIEMNPRVS RSSALASKAT GYPIAKMAAK LAIGYTLDEI VNDITKETPA CFEPTLDYVV 

       370        380        390        400        410        420 
VKAPRFAFEK FPGADGTLTT TMKSVGEAMS IGRNFTEAFG KVLRSLETKR AGYWTGPEVE 

       430        440        450        460        470        480 
GTLDELLEAI KVPTDGRMYQ IAQAFELGAT LEQLFDATAI DPWFLDQMQQ IVELGAEVRS 

       490        500        510        520        530        540 
AETFGATELR FAKHHGFSDR QIAALRPQQF GEGQAGEDAV RALRDELNVH PVYKTVDTCA 

       550        560        570        580        590        600 
AEFEAKTPYH YSTYELDPEA ETEVAPQTER PKVLILGSGP NRIGQGIEFD YSCVHAAQTL 

       610        620        630        640        650        660 
SEAGYETVMV NCNPETVSTD YDTADRLYFE PLTFEDVLEV YRAETLSGTV AGVIVQLGGQ 

       670        680        690        700        710        720 
TPLGLAKRLK AAGVPIVGTS PEAIDLAEDR GEFGRVLTEA GLPAPKFGTA TTFEGAREIA 

       730        740        750        760        770        780 
SGIGYPVLVR PSYVLGGRGM EIVYDEKALE SYISRATEIS DDRPVLVDRF LEDAVEIDVD 

       790        800        810        820        830        840 
ALCDGTEVYL GGVMEHIEEA GIHSGDSACA LPPITLGRAD LENVRRSTEA LAKGIGVKGL 

       850        860        870        880        890        900 
LNVQYALKDD ILYVLEANPR ASRTVPFVSK ATAVQLAKAC ARVMLGESIA DLRAGGILPA 

       910        920        930        940        950        960 
EGDGGHAPID APVAVKEAVL PFNRFRRADG TGIDTLLSPE MKSTGEVMGI DADFGTAFAK 

       970        980        990       1000       1010       1020 
SQTAAYGSLP TSGSVFVSVA NKDKRSLIFP VKRLADLGFR ILATEGTADV LRRNGITCEE 

      1030       1040       1050       1060       1070       1080 
VHKQSGENLP EGARTIVDQI KDGEVDMVIN TPYGNSGPRV DGYEIRSAAV SKSVPCITTV 

      1090       1100       1110 
QGASAAVQGI EAAIRGDIGV QSLQELHTRL RDQQQ 

« Hide

References

[1]"The genome of a pathogenic rhodococcus: cooptive virulence underpinned by key gene acquisitions."
Letek M., Gonzalez P., Macarthur I., Rodriguez H., Freeman T.C., Valero-Rello A., Blanco M., Buckley T., Cherevach I., Fahey R., Hapeshi A., Holdstock J., Leadon D., Navas J., Ocampo A., Quail M.A., Sanders M., Scortti M.M. expand/collapse author list , Prescott J.F., Fogarty U., Meijer W.G., Parkhill J., Bentley S.D., Vazquez-Boland J.A.
PLoS Genet. 6:E1001145-E1001145(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 103S.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN563149 Genomic DNA. Translation: CBH48221.1.
RefSeqYP_004006905.1. NC_014659.1.

3D structure databases

ProteinModelPortalE4WH16.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBH48221; CBH48221; REQ_21680.
GeneID9966933.
KEGGreq:REQ_21680.
PATRIC42661759. VBIRhoEqu141084_2164.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000234582.
KOK01955.
OMATFIDKWF.

Enzyme and pathway databases

BioCycREQU685727:GHKP-2094-MONOMER.
UniPathwayUPA00068; UER00171.
UPA00070; UER00115.

Family and domain databases

Gene3D1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
HAMAPMF_01210_B. CPSase_L_chain_B.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE4WH16_RHOE1
AccessionPrimary (citable) accession number: E4WH16
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: June 11, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)