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B1YMV8 (B1YMV8_BURA4) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 49. 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
Ordered Locus Names:BamMC406_1181 EMBL ACB63672.1
OrganismBurkholderia ambifaria (strain MC40-6) [Complete proteome] [HAMAP] EMBL ACB63672.1
Taxonomic identifier398577 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length1084 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 SAAS006275 HAMAP-Rule MF_01210

Cofactor

Binds 4 magnesium or manganese ions per subunit By similarity. HAMAP-Rule MF_01210 SAAS SAAS006275

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. SAAS SAAS006275 HAMAP-Rule MF_01210

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. SAAS SAAS006275 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. HAMAP-Rule MF_01210 SAAS SAAS006275

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 – 335203ATP-grasp 1 By similarity HAMAP-Rule MF_01210
Domain680 – 880201ATP-grasp 2 By similarity HAMAP-Rule MF_01210
Nucleotide binding166 – 22358ATP By similarity HAMAP-Rule MF_01210
Nucleotide binding706 – 76358ATP By similarity HAMAP-Rule MF_01210
Region1 – 410410Carboxyphosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region411 – 555145Oligomerization domain By similarity HAMAP-Rule MF_01210
Region556 – 946391Carbamoyl phosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region947 – 1084138Allosteric domain By similarity HAMAP-Rule MF_01210

Sites

Metal binding2921Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding3061Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding3061Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding3081Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding8301Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8511Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8511Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210
Metal binding8531Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210

Sequences

Sequence LengthMass (Da)Tools
B1YMV8 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 03C125233E06ED28

FASTA1,084118,534
        10         20         30         40         50         60 
MPKRTDIKSI LIIGAGPIII GQACEFDYSG AQACKALREE GYKVVLVNSN PATIMTDPNT 

        70         80         90        100        110        120 
ADVTYIEPIT WEVVARIIEK ERPDAILPTM GGQTALNCAL DLHHHGVLEK FGVELIGASP 

       130        140        150        160        170        180 
EAIDKAEDRQ KFKDAMTKIG LGSAKSGIAH SMEEATQVHA EIMAYTGGSG YPVVIRPSFT 

       190        200        210        220        230        240 
LGGSGGGIAY NREEFEEICK RGLDLSPTRE LLIEESLLGW KEYEMEVVRD RADNCIIVCS 

       250        260        270        280        290        300 
IENLDPMGVH TGDSITVAPA QTLTDKEYQI LRNASLAVLR EIGVDTGGSN VQFSINPKDG 

       310        320        330        340        350        360 
RMVVIEMNPR VSRSSALASK ATGFPIAKVA AKLAVGYTLD ELKNEITGGQ TPASFEPTID 

       370        380        390        400        410        420 
YVVTKIPRFA FEKFREADSR LTTQMKSVGE VMAIGRTFQE SFQKALRGLE VGVDGLDEKS 

       430        440        450        460        470        480 
TDRDEIAIEI HEPGPDRIWY VGDAFRIGMT AEEIFAETAI DPWFLAQIEQ IILKEKALSG 

       490        500        510        520        530        540 
RTLASLTFDE LRFLKQSGFS DRRLAKLLGA TPEDVRKRRV ELNVRPVYKR VDTCAAEFAT 

       550        560        570        580        590        600 
KTAYMYSTYE EECEAQPTTN KKIMVLGGGP NRIGQGIEFD YCCVHAALAM REDGYETIMV 

       610        620        630        640        650        660 
NCNPETVSTD YDTSDRLYFE PLTLEDVLEI VDKEKPVGVI VQYGGQTPLK LALDLEAHGV 

       670        680        690        700        710        720 
PIVGTSPDMI DAAEDRERFQ KLLQDLGLRQ PPNRTARAEE EALALAAEIG YPLVVRPSYV 

       730        740        750        760        770        780 
LGGRAMEIVH EPRDLERYMR EAVKVSNDSP VLLDRFLNDA IECDVDCICD GEAVFIGGVM 

       790        800        810        820        830        840 
EHIEQAGVHS GDSACSLPPY SLSKETVAEL KRQTGAMAKA LNVVGLMNVQ FAIQQVPQAD 

       850        860        870        880        890        900 
GSKQDIIYVL EVNPRASRTV PYVSKATSLP LAKIAARAMV GQKLAQQGVT KEVEPPYFSV 

       910        920        930        940        950        960 
KEAVFPFVKF PTVDPVLGPE MRSTGEVMGV GQTFGEALFK SQLAAGSRLP ESGTVLLTVM 

       970        980        990       1000       1010       1020 
DADKPKAVEV ARMLHDLGYP IVATKGTAAA IEAAGVPVKV VNKVKDGRPH IVDMIKNGEI 

      1030       1040       1050       1060       1070       1080 
ALVFTTVDET RQAIADSRSI RMSAQAHKVT YYTTMSGARA AVEGLRYLKD LEVYDLQGLH 


ARLN 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Ramette A., Konstantinidis K., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC40-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001025 Genomic DNA. Translation: ACB63672.1.
RefSeqYP_001807888.1. NC_010551.1.

3D structure databases

ProteinModelPortalB1YMV8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398577.BamMC406_1181.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB63672; ACB63672; BamMC406_1181.
GeneID6178800.
KEGGbac:BamMC406_1181.
PATRIC19031760. VBIBurAmb82852_1213.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0458.
HOGENOMHOG000234582.
KOK01955.
OMARLVVIEM.
OrthoDBEOG6J1DC6.
ProtClustDBPRK05294.

Enzyme and pathway databases

BioCycBAMB398577:GH38-1218-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. 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 nameB1YMV8_BURA4
AccessionPrimary (citable) accession number: B1YMV8
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)