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F0T029 (F0T029_SYNGF) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | 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 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
Ordered Locus Names:Sgly_0678 EMBL ADY55040.1
OrganismSyntrophobotulus glycolicus (strain DSM 8271 / FlGlyR) [Complete proteome] [HAMAP] EMBL ADY55040.1
Taxonomic identifier645991 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Syntrophobotulus ›

Protein attributes

Sequence length1062 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 SAAS SAAS005483

Cofactor

Binds 4 magnesium or manganese ions per subunit By similarity. HAMAP-Rule MF_01210 SAAS SAAS005483

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP-Rule MF_01210 SAAS SAAS005483

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP-Rule MF_01210 SAAS SAAS005483

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 SAAS005483

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

Domain132 – 326195ATP-grasp 1 By similarity HAMAP-Rule MF_01210
Domain670 – 860191ATP-grasp 2 By similarity HAMAP-Rule MF_01210
Nucleotide binding158 – 21558ATP By similarity HAMAP-Rule MF_01210
Nucleotide binding696 – 75358ATP By similarity HAMAP-Rule MF_01210
Region1 – 400400Carboxyphosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region401 – 545145Oligomerization domain By similarity HAMAP-Rule MF_01210
Region546 – 928383Carbamoyl phosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region929 – 1062134Allosteric domain By similarity HAMAP-Rule MF_01210

Sites

Metal binding2831Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding2971Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding2971Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding2991Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding8191Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8311Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8311Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210
Metal binding8331Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210

Sequences

Sequence LengthMass (Da)Tools
F0T029 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: FDFE6A5492A11C9C

FASTA1,062116,389
        10         20         30         40         50         60 
MPKKDWKKVM VIGSGPIVIG QAAEFDYAGT QACRALREEG LETVLVNSNP ATIMTDAEVA 

        70         80         90        100        110        120 
DKIYIEPLTI EFLERIIEKE KPDGLLPTMG GQTGLNLAFQ LSQSGILQRC GVTLLGTPLD 

       130        140        150        160        170        180 
SISKAEDREH FRNLMHEIRQ PIPESTIVSE VGEAVAFAEE IGYPLIVRPA FTLGGTGGGI 

       190        200        210        220        230        240 
AGDRKTLEEI AASGINASMI GQILIERSVA GWKEIEFEVL RDGMDSCIAV CHMENMDPVG 

       250        260        270        280        290        300 
VHTGDSIVVA PCQTLTDKEI QMLRTASFNI VSALGIEGGC NVQFALNPVN DEYYVIEVNP 

       310        320        330        340        350        360 
RLSRSSALAS KATGYPIAKI AAKIGIGYTM AELKNSVTGK TSACFEPALD YVVVKIPRWP 

       370        380        390        400        410        420 
FDKFSDADRT LGTQMKATGE VMGLGRNLET ALLKAVRSLE TKSFGILNPE NERLADRELE 

       430        440        450        460        470        480 
AKCAQASDNM LYLIAEGFRR GWSVEKINRI NQWNPYFLKI IQRIVDFSAE IKNHPWDGAI 

       490        500        510        520        530        540 
LRKAKKLGFA DQNIARLWAA EEEKVFAFRR ENGLLPVFKM VDTCAGEFDA MTPYFYSSYD 

       550        560        570        580        590        600 
QEDEGEVTSR RKVVVLGSGP IRIGQGIEFD YCSVHAVKAL RKAGVESIII NNNPETVSTD 

       610        620        630        640        650        660 
FDTSDRLYFE PLTLEDVSEV LNKEKPEGVI VQFGGQTAIG LCKGLAARGY RILGTTVEDT 

       670        680        690        700        710        720 
DRAEERGIFD HVLQELGAKR PQGGCVSTVE EAEKLSEKIG FPLIVRPSYV LGGRAMQIVY 

       730        740        750        760        770        780 
DRADIKRIVQ NAFAEFPGQQ IWMDQYLEGK EVEVDAISDG ETVCIPGIME HLERAGVHSG 

       790        800        810        820        830        840 
DSIAVYPPQT LAQKMENRIS DLTVSIARSL RIKGLLNIQY VIYKDEVYVL EVNPRSSRTV 

       850        860        870        880        890        900 
PFLSKVTGVP VVDLATRVIL GQSLASMGIS SGVWPKSSYV AVKAPVFSFS KLLMVEPSLG 

       910        920        930        940        950        960 
PEMKSTGEVM GTDSTYEKAL HKALLAAGMH ISAHGTLLVT LADRDKAEGL QLVRRFYDLG 

       970        980        990       1000       1010       1020 
FHIVATAGTA RAIEKEGLEV EEVRKIYTGS NEITEKIKGG QIQCVLNTTT HAKNTTSDGF 

      1030       1040       1050       1060 
AIRRAAVEQG IPCFTSLDTA QALLQVLEAN SPSIIPLNEK RF

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References

[1]"The complete genome of Syntrophobotulus glycolicus DSM 8271."
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L. expand/collapse author list , Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 8271 / FlGlyR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002547 Genomic DNA. Translation: ADY55040.1.
RefSeqYP_004265041.1. NC_015172.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY55040; ADY55040; Sgly_0678.
GeneID10247858.
KEGGsgy:Sgly_0678.
PATRIC47031962. VBISynGly105927_0711.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01955.

Enzyme and pathway databases

BioCycSGLY645991:GHJ4-704-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 nameF0T029_SYNGF
AccessionPrimary (citable) accession number: F0T029
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: April 3, 2013
This is version 17 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