Skip Header

Contribute Send feedback
Read comments (?) or add your own

B7UI78 (B7UI78_ECO27) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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 CAS07581.1
Ordered Locus Names:E2348C_0033 EMBL CAS07581.1
OrganismEscherichia coli O127:H6 (strain E2348/69 / EPEC) [Complete proteome] [HAMAP]
Taxonomic identifier574521 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length1073 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 SAAS005481 HAMAP-Rule MF_01210

Cofactor

Binds 4 magnesium or manganese ions per subunit By similarity. SAAS SAAS005481 HAMAP-Rule MF_01210

Pathway

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

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. SAAS SAAS005481 HAMAP-Rule MF_01210

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. SAAS SAAS005481 HAMAP-Rule MF_01210

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

Domain133 – 328196ATP-grasp 1 By similarity HAMAP-Rule MF_01210
Domain679 – 870192ATP-grasp 2 By similarity HAMAP-Rule MF_01210
Nucleotide binding159 – 21658ATP By similarity HAMAP-Rule MF_01210
Nucleotide binding705 – 76258ATP By similarity HAMAP-Rule MF_01210
Region1 – 403403Carboxyphosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region404 – 553150Oligomerization domain By similarity HAMAP-Rule MF_01210
Region554 – 936383Carbamoyl phosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region937 – 1073137Allosteric domain By similarity HAMAP-Rule MF_01210

Sites

Metal binding2851Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding2991Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding2991Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding3011Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding8291Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8411Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8411Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210
Metal binding8431Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210

Sequences

Sequence LengthMass (Da)Tools
B7UI78 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 13B30A1A3916A193

FASTA1,073117,900
        10         20         30         40         50         60 
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM 

        70         80         90        100        110        120 
ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA 

       130        140        150        160        170        180 
DAIDKAEDRR RFDVAMKKIG LETARSGIAH SMEEALAVAA EVGFPCIIRP SFTMGGSGGG 

       190        200        210        220        230        240 
IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM 

       250        260        270        280        290        300 
GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM 

       310        320        330        340        350        360 
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP 

       370        380        390        400        410        420 
RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA 

       430        440        450        460        470        480 
LTKIRRELKD AGAERIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG 

       490        500        510        520        530        540 
ITGLNAEFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT 

       550        560        570        580        590        600 
AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN 

       610        620        630        640        650        660 
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP 

       670        680        690        700        710        720 
VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTTIEM AVEKAKEIGY PLVVRPSYVL 

       730        740        750        760        770        780 
GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME 

       790        800        810        820        830        840 
HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI 

       850        860        870        880        890        900 
EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF 

       910        920        930        940        950        960 
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL 

       970        980        990       1000       1010       1020 
AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR 

      1030       1040       1050       1060       1070 
RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK

« Hide

References

[1]"Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69."
Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.
J. Bacteriol. 191:347-354(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E2348/69 / EPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM180568 Genomic DNA. Translation: CAS07581.1.
RefSeqYP_002327625.1. NC_011601.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING574521.E2348C_0033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS07581; CAS07581; E2348C_0033.
GeneID7064324.
KEGGecg:E2348C_0033.
PATRIC18338961. VBIEscCol90278_0034.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0458.
HOGENOMHOG000234582.
KOK01955.
OMAPMANLAT.
ProtClustDBPRK05294.

Enzyme and pathway databases

BioCycECOL574521:GJAO-34-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_A. CPSase_L_chain_A.
MF_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. CarbamoylP_synth_lsu_oligo. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
SSF52440. PreATP-grasp-like. 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 nameB7UI78_ECO27
AccessionPrimary (citable) accession number: B7UI78
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info