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E1RG39 (E1RG39_METP4) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 22. 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:Mpet_1517
OrganismMethanoplanus petrolearius (strain DSM 11571 / OCM 486 / SEBR 4847) [Complete proteome] [HAMAP] EMBL ADN36274.1
Taxonomic identifier679926 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanomicrobiales › Methanomicrobiaceae › Methanoplanus ›

Protein attributes

Sequence length1055 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. 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. 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

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

Domain131 – 323193ATP-grasp 1 By similarity HAMAP-Rule MF_01210
Domain662 – 853192ATP-grasp 2 By similarity HAMAP-Rule MF_01210
Nucleotide binding157 – 21458ATP By similarity HAMAP-Rule MF_01210
Nucleotide binding688 – 74558ATP By similarity HAMAP-Rule MF_01210
Region1 – 397397Carboxyphosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region398 – 531134Oligomerization domain By similarity HAMAP-Rule MF_01210
Region532 – 920389Carbamoyl phosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region921 – 1055135Allosteric domain By similarity HAMAP-Rule MF_01210

Sites

Metal binding2821Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding2941Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding2941Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding2961Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding8121Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8241Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8241Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210
Metal binding8261Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210

Sequences

Sequence LengthMass (Da)Tools
E1RG39 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: EC5F93015CC0E6D1

FASTA1,055116,025
        10         20         30         40         50         60 
MPRREDIKKV ILIGSGPIQI GQAAEFDFSG SQACRALREE GVEVVLVNSN PATIQTDPDT 

        70         80         90        100        110        120 
ADVVYVEPLK AGIIAKIIEK EKPDGILSGM GGQTGLNLTA ELAEMGALED VEILGTPLEA 

       130        140        150        160        170        180 
IYKGEDREKF RDLMNDIGEP IPRSMILRSM DQLDNALEIV GLPAIIRPAY TLGGAGGGVA 

       190        200        210        220        230        240 
HTPEELRKIV EIGLQRSRIH QVLIEESVMG WKEIEYEVMR DSFDTCLIVC GMENVDAMGI 

       250        260        270        280        290        300 
HTGESVVVAP ILTLTDEEFH LLRTAAIKII RALDVQGGCN IQMAFKDGDY RIIEVNPRVS 

       310        320        330        340        350        360 
RSSALASKAT GYPIARVAAK IAIGLRLDEI MNSVTGCTPA SFEPSIDYVV VKIPRWPFDK 

       370        380        390        400        410        420 
FKNADRTLTT AMKSTGEVMS IGRTLEEAFM KAMRSLDTDI NSHTDKDEIR MLLQNPTDER 

       430        440        450        460        470        480 
FGCLFDAFRQ GFTVEEVSAL TFIDVFFLQK IENLVEIEKK LKSGSVSEDD IRNAVHYGFS 

       490        500        510        520        530        540 
VTEIGELTGK PEKEIEAIAG LPVYKLVDTC AAEFPAKTPY FYSTRDEGCE IDRDGKQKIL 

       550        560        570        580        590        600 
ILGSGPIRIG QGIEFDYCTV HAVMALREEG IEVHIVNNNP ETVSTDFDTS DRLFFEPMKL 

       610        620        630        640        650        660 
EDVMNILRKD DYYGVMVQFG GQNSVNLATS IEEKIKEYGL KTKILGTSPA AMDLAEDRDQ 

       670        680        690        700        710        720 
FSRLLERLDI PSPANGSAHS ETEAMQVAKK IGYPLLVRPS YVLGGRAMEL VHDDIELRNY 

       730        740        750        760        770        780 
IKEAVKVSRK HPVLLDSFLQ NAIEIDVDAV CDGEDVLIGG IMEHIEEAGV HSGDSACVIP 

       790        800        810        820        830        840 
SQSLSKNVIA TVKDYTRKLA LGIGVVGLIN IQYAVKDEVV YVLEANPRAS RTVPFVSKAT 

       850        860        870        880        890        900 
GIPLAKIAAR VMTDGKLKTY GITEKKLSHV SVKEVLLPFN KLPGVDITLS PEMKSTGEVM 

       910        920        930        940        950        960 
GIDYDFGRAY YKACISAENQ LPLEGKVFIS AGSEFKQDFV PIAKKLCSLG LSIVGTKGTV 

       970        980        990       1000       1010       1020 
ETLRENGIEA DLVRKVQEGS PNVIDFMRRG EINLIINTPS GKYSRQDHMQ IMRAALDYNT 

      1030       1040       1050 
PYITTIQAAK AAAMAIESMK KGDITIEPLS HYHEN

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002117 Genomic DNA. Translation: ADN36274.1.
RefSeqYP_003894712.1. NC_014507.1.

3D structure databases

ProteinModelPortalE1RG39.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADN36274; ADN36274; Mpet_1517.
GeneID9743987.
KEGGmpi:Mpet_1517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000234582.
KOK01955.
OMAPMANLAT.

Enzyme and pathway databases

BioCycMPET679926:GHOF-1550-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. 1 hit.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE1RG39_METP4
AccessionPrimary (citable) accession number: E1RG39
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: May 1, 2013
This is version 22 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