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O25577 (CARB_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase large chain

EC=6.3.5.5
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene names
Name:carB
Ordered Locus Names:HP_0919
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length1085 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. HAMAP-Rule MF_01210

Cofactor

Binds 4 magnesium or manganese ions per subunit By similarity.

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. 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.

Sequence similarities

Belongs to the CarB family.

Contains 2 ATP-grasp domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10851085Carbamoyl-phosphate synthase large chain HAMAP-Rule MF_01210
PRO_0000145010

Regions

Domain131 – 326196ATP-grasp 1
Domain678 – 871194ATP-grasp 2
Nucleotide binding157 – 21458ATP By similarity
Nucleotide binding704 – 76461ATP By similarity
Region1 – 399399Carboxyphosphate synthetic domain HAMAP-Rule MF_01210
Region400 – 552153Oligomerization domain HAMAP-Rule MF_01210
Region553 – 951399Carbamoyl phosphate synthetic domain HAMAP-Rule MF_01210
Region952 – 1085134Allosteric domain HAMAP-Rule MF_01210

Sites

Metal binding2831Magnesium or manganese 1 By similarity
Metal binding2971Magnesium or manganese 1 By similarity
Metal binding2971Magnesium or manganese 2 By similarity
Metal binding2991Magnesium or manganese 2 By similarity
Metal binding8301Magnesium or manganese 3 By similarity
Metal binding8421Magnesium or manganese 3 By similarity
Metal binding8421Magnesium or manganese 4 By similarity
Metal binding8441Magnesium or manganese 4 By similarity

Sequences

Sequence LengthMass (Da)Tools
O25577 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 696E124A50DB34C1

FASTA1,085120,074
        10         20         30         40         50         60 
MPKRTDISNI LLIGSGPIVI GQACEFDYSG TQSCKTLKSL GYRVILINSN PATVMTDPEF 

        70         80         90        100        110        120 
SHQTYIQPIT PENIATIIEK EKIDAILPTM GGQTALNAVM QMHQKGMLEG VELLGAKIEA 

       130        140        150        160        170        180 
IKKGEDRQAF KEAMLKIGMD LPKGRYAYTE LEALEAINEI GFPAIIRASF TLAGGGSGVA 

       190        200        210        220        230        240 
YNIEEFQELA KNALDASPIN EILIEESLLG WKEYEMEVIR DSKDNCIIVC CIENIDPMGV 

       250        260        270        280        290        300 
HTGDSITIAP SLTLTDKEYQ RMRDASFAIL REIGVDTGGS NVQFAIHPET LRMVVIEMNP 

       310        320        330        340        350        360 
RVSRSSALAS KATGFPIAKV ATMLAVGFSL DEIQNDITNT PASFEPSLDY IVVKIPRFAF 

       370        380        390        400        410        420 
EKFAGVSSTL GTSMKSIGEV MAIGGNFLEA LQKALCSLEN NWLGFESLSK DLEAIKKEIR 

       430        440        450        460        470        480 
RPNPKRLLYI ADAFRLGVCV DEVFELCQID RWFLSQIQKL VEVEESINSS VLTDAKKLRG 

       490        500        510        520        530        540 
LKNLGFSDAR IAAKIKENEN LEVSPFEVEL ARSNLQIVPN FEEVDTCAAE FLSLTPYLYS 

       550        560        570        580        590        600 
TYAPNPLPPI ENKQEKKEKK ILIIGSGPNR IGQGIEFDYC CVHASLALKD LNIKSVMFNC 

       610        620        630        640        650        660 
NPETVSTDYD TSDTLYFEPI HFECVKSIIQ RERVDGIIVH FGGQTPLKLA KDLAKMQAPI 

       670        680        690        700        710        720 
IGTPFKVIDI AEDREKFSLF LKELDIKQPK NGMAKSVDEA YSIANVIGFP IIVRPSYVLG 

       730        740        750        760        770        780 
GQHMQILENI EELRHYLESV THALEISPKN PLLIDKFLEK AVELDVDAIC DKKEVYIAGI 

       790        800        810        820        830        840 
LQHIEEAGIH SGDSACFIPS TLSPEILDEI ERVSAKIALH LGVVGLLNIQ FAVHQNSLYL 

       850        860        870        880        890        900 
IEVNPRASRT VPFLSKALGV PLAKVATRVM VLEDLKEALK FYDKKNIVGY SKGVYKPKMP 

       910        920        930        940        950        960 
HFVALKEAVF PFNKLYGSDL ILGPEMKSTG EVMGIARSLG LAFFKAQTAC FNPIKNKGLI 

       970        980        990       1000       1010       1020 
FVSIKDKDKE EACVLMKRLV QLGFELCATE GTHKALEKAG VKSLKVLKIS EGRPNIMDLM 

      1030       1040       1050       1060       1070       1080 
MNGEISMAIN TSDHKSQDDA KLIRASVLKN HVSYFTTLST IEVLLLALEE SSKEDELLAL 


QDYLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD07963.1.
PIRG64634.
RefSeqNP_207711.1. NC_000915.1.
YP_006934834.1. NC_018939.1.

3D structure databases

ProteinModelPortalO25577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-3181N.
IntActO25577. 6 interactions.
MINTMINT-187278.
STRING85962.HP0919.

Proteomic databases

PRIDEO25577.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07963; AAD07963; HP_0919.
GeneID13870106.
899448.
KEGGheo:C694_04730.
hpy:HP0919.
PATRIC20593139. VBIHelPyl33062_0955.

Phylogenomic databases

eggNOGCOG0458.
KOK01955.
OMARLVVIEM.
OrthoDBEOG6J1DC6.
ProtClustDBPRK05294.

Enzyme and pathway databases

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.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARB_HELPY
AccessionPrimary (citable) accession number: O25577
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names