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Q8ZIL4 (CARB_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:YPO0482, y3692, YP_3697
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length1077 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Initiator methionine11Removed By similarity
Chain2 – 10771076Carbamoyl-phosphate synthase large chain HAMAP-Rule MF_01210
PRO_0000145069

Regions

Domain133 – 328196ATP-grasp 1
Domain679 – 870192ATP-grasp 2
Nucleotide binding159 – 21658ATP By similarity
Nucleotide binding705 – 76258ATP By similarity
Region2 – 403402Carboxyphosphate synthetic domain HAMAP-Rule MF_01210
Region404 – 553150Oligomerization domain HAMAP-Rule MF_01210
Region554 – 936383Carbamoyl phosphate synthetic domain HAMAP-Rule MF_01210
Region937 – 1077141Allosteric domain HAMAP-Rule MF_01210

Sites

Metal binding2851Magnesium or manganese 1 By similarity
Metal binding2991Magnesium or manganese 1 By similarity
Metal binding2991Magnesium or manganese 2 By similarity
Metal binding3011Magnesium or manganese 2 By similarity
Metal binding8291Magnesium or manganese 3 By similarity
Metal binding8411Magnesium or manganese 3 By similarity
Metal binding8411Magnesium or manganese 4 By similarity
Metal binding8431Magnesium or manganese 4 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZIL4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0D4604F55EA55D9F

FASTA1,077118,244
        10         20         30         40         50         60 
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN LATIMTDPEM 

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

       130        140        150        160        170        180 
DAIDKAEDRR RFDIAMKKIG LDTARSGIAH NMEEALAVAA DVGFPCIIRP SFTMGGTGGG 

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

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

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

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

       430        440        450        460        470        480 
LTKIRRELKE AGAERIWYIA DAFRAGMSVD GVFNLTNVDR WFLVQIEELV RLEESVAELG 

       490        500        510        520        530        540 
INGLTAEFMR HLKRKGFADA RLAKLVGAAE SEVRKLRYKY GLHPVYKRVD TCAAEFSTDT 

       550        560        570        580        590        600 
AYMYSTYEEE CESNPTSDRP KVMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN 

       610        620        630        640        650        660 
CNPETVSTDY DTSDRLYFES VTLEDVLEIV RIEKPQGVIV QYGGQTPLKL ARELEAAGVP 

       670        680        690        700        710        720 
IIGTSPDAID RAEDRERFQQ AVNRLGLKQP ANATVATIEQ AVEKATGLGY PLVVRPSYVL 

       730        740        750        760        770        780 
GGRAMEIVYD EIDLRRYFQN AVSVSNDAPV LLDRFLDDAV EVDVDAICDG ERVLIGGIME 

       790        800        810        820        830        840 
HIEQAGVHSG DSACSLPAYT LSKEIQDVMR QQVEKLAFEL CVRGLMNVQF AVKNNEVYLI 

       850        860        870        880        890        900 
EVNPRAARTV PFVSKATGMP LAKIAARVMV GQSLAEQGML EEIIPPYYSV KEVVLPFNKF 

       910        920        930        940        950        960 
PGVDPILGPE MRSTGEVMGV GRTFAEAFSK AMLGSQSGMK KSGRALLSVR EGDKHRVVDL 

       970        980        990       1000       1010       1020 
AAKLLKQGFE LDATHGTAVV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIVNTTAGR 

      1030       1040       1050       1060       1070 
QAIEDSKLIR RSALQYKVHY DTTLNGGFAT AMALNADPTD QVISVQEMHA KIKNMKA

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References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL590842 Genomic DNA. Translation: CAL19162.1.
AE009952 Genomic DNA. Translation: AAM87240.1.
AE017042 Genomic DNA. Translation: AAS63845.1.
PIRAH0059.
RefSeqNP_670989.1. NC_004088.1.
NP_994968.1. NC_005810.1.
YP_002345555.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ8ZIL4.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8ZIL4. 8 interactions.
STRING214092.YPO0482.

Proteomic databases

PRIDEQ8ZIL4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM87240; AAM87240; y3692.
AAS63845; AAS63845; YP_3697.
GeneID1148639.
1173327.
2766698.
KEGGype:YPO0482.
ypk:y3692.
ypm:YP_3697.

Phylogenomic databases

eggNOGCOG0458.
HOGENOMHOG000234582.
KOK01955.
OMAPMANLAT.
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. 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 nameCARB_YERPE
AccessionPrimary (citable) accession number: Q8ZIL4
Secondary accession number(s): Q0WJI3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents