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D3PQ55 (D3PQ55_MEIRD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 28. 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:Mrub_0916
OrganismMeiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus ruber) [Complete proteome] [HAMAP]
Taxonomic identifier504728 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Meiothermus ›

Protein attributes

Sequence length1038 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 SAAS005481 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

Domain133 – 329197ATP-grasp 1 By similarity HAMAP-Rule MF_01210
Domain692 – 884193ATP-grasp 2 By similarity HAMAP-Rule MF_01210
Nucleotide binding160 – 21758ATP By similarity HAMAP-Rule MF_01210
Nucleotide binding718 – 77659ATP By similarity HAMAP-Rule MF_01210
Region1 – 411411Carboxyphosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region412 – 554143Oligomerization domain By similarity HAMAP-Rule MF_01210
Region555 – 950396Carbamoyl phosphate synthetic domain By similarity HAMAP-Rule MF_01210
Region951 – 103888Allosteric domain By similarity HAMAP-Rule MF_01210

Sites

Metal binding2861Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding3001Magnesium or manganese 1 By similarity HAMAP-Rule MF_01210
Metal binding3001Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding3021Magnesium or manganese 2 By similarity HAMAP-Rule MF_01210
Metal binding8431Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8551Magnesium or manganese 3 By similarity HAMAP-Rule MF_01210
Metal binding8551Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210
Metal binding8571Magnesium or manganese 4 By similarity HAMAP-Rule MF_01210

Sequences

Sequence LengthMass (Da)Tools
D3PQ55 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: A3DA9A98A1E25318

FASTA1,038113,358
        10         20         30         40         50         60 
MPARTDLKKI MIIGSGPITI GQAAEFDYSG TQAVKALRSV GYQVVLVNSN PATIMTDPEL 

        70         80         90        100        110        120 
AEGTYLEPLT VEFLEKIIAA ERPDALLPTL GGQTALNLSM ALYEQGILEK YGVELIGANA 

       130        140        150        160        170        180 
AAIKKGEDRE EFQKAMLKIG VDVPRGKMVH SLEEGLAFAR EVTGYPVVVR PSFTLGGTGG 

       190        200        210        220        230        240 
GIAENEAEFV EILSRGLSLS PTHSALVEES IVGWKEYELE VMRDKNDTVV IITSIENLDP 

       250        260        270        280        290        300 
MGVHTGDSIT VAPAQTLSDV EYQRMRDAAI AIIREIGVET GGSNIQFAID PKSGRMIVIE 

       310        320        330        340        350        360 
MNPRVSRSSA LASKATGFPI AKIAALLAVG YTLDEIPNDI TQKTPASFEP TIDYVVTKIP 

       370        380        390        400        410        420 
RFAFEKFSTL PNTNPGGFSD RLGTQMKSVG EVMAIGRTFK ESFGKALRSL EADVRSEFSG 

       430        440        450        460        470        480 
LTTEELEARL YPSPTRIYAV LELLRRGVQV DHLYEKTKIE PWFLTQLKEV VEAEHDLETE 

       490        500        510        520        530        540 
PHRLEDLEDW RYVKGLGLSD ARVGELLGVS EAAARKQRLA AGCKPVYKTV DTCAAEFEAY 

       550        560        570        580        590        600 
TPYHYSTYEL EDEVRPTSKP KVVILGSGPI RIGQGVEFDY ATVHAVWALR EAAIPPERPG 

       610        620        630        640        650        660 
EAGARGYETI MVNSNPETVS TDYDTADRLY FEPLTLEDVL NLAEHEKPIG VIATLGGQTP 

       670        680        690        700        710        720 
LKLAKKLAEA GVPLLGTSWE AIHKAEDRAE FNQLCAALGI PQPKGAVART PEEALKLAET 

       730        740        750        760        770        780 
LGYPLMARPS YVLGGRAMQV VRNPEELRWY LSGIYAALAE RPSILLDQYL ENALELDVDA 

       790        800        810        820        830        840 
LCDGKQVVVA GIMEHIERAG VHSGDSATIL PPISLTPEQL ETVKAYTRKL ALAVGVRGLI 

       850        860        870        880        890        900 
NVQYAIKDGV VYILEANPRA SRTVPFVSKA IGHPLAKYAA LIAVGHTLEE LGFTQDPTPS 

       910        920        930        940        950        960 
FYAVKEVLIP WLKFPGVIPV LGPEMRSTGE SMGIDTDPYL AYYRAELGVG QRLPLSGKVR 

       970        980        990       1000       1010       1020 
FIGAEQLKPD WEAAGFEVSE GDYDLLIALT PDPELRRAVE TGKPFITTLE GARWSLEAIL 

      1030 
RARHSNLPVR SLQAWHGR

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001743 Genomic DNA. Translation: ADD27681.1.
RefSeqYP_003506701.1. NC_013946.1.

3D structure databases

ProteinModelPortalD3PQ55.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADD27681; ADD27681; Mrub_0916.
GeneID8879003.
KEGGmrb:Mrub_0916.
PATRIC35357964. VBIMeiRub128672_0920.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000234582.
KOK01955.
OMAPMANLAT.

Enzyme and pathway databases

BioCycMRUB504728:GI6U-937-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.
3.40.50.20. 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.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMSSF48108. CarbamoylP_synth_lsu_oligo. 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 nameD3PQ55_MEIRD
AccessionPrimary (citable) accession number: D3PQ55
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: May 1, 2013
This is version 28 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