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Q8DZQ7 (CARB_STRA5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:SAG1042
OrganismStreptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R) [Complete proteome] [HAMAP]
Taxonomic identifier208435 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length1060 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.

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

Chain1 – 10601060Carbamoyl-phosphate synthase large chain HAMAP-Rule MF_01210
PRO_0000145048

Regions

Domain133 – 327195ATP-grasp 1
Domain671 – 861191ATP-grasp 2
Nucleotide binding159 – 21658ATP By similarity
Nucleotide binding697 – 75458ATP By similarity
Region1 – 401401Carboxyphosphate synthetic domain HAMAP-Rule MF_01210
Region402 – 546145Oligomerization domain HAMAP-Rule MF_01210
Region547 – 929383Carbamoyl phosphate synthetic domain HAMAP-Rule MF_01210
Region930 – 1060131Allosteric domain HAMAP-Rule MF_01210

Sites

Metal binding2841Magnesium or manganese 1 By similarity
Metal binding2981Magnesium or manganese 1 By similarity
Metal binding2981Magnesium or manganese 2 By similarity
Metal binding3001Magnesium or manganese 2 By similarity
Metal binding8201Magnesium or manganese 3 By similarity
Metal binding8321Magnesium or manganese 3 By similarity
Metal binding8321Magnesium or manganese 4 By similarity
Metal binding8341Magnesium or manganese 4 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DZQ7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 04C6D2B617E08274

FASTA1,060117,093
        10         20         30         40         50         60 
MPKRTDIRKI MVIGSGPIVI GQAAEFDYSG TQACLSLKEE GYQVVLVNSN PATIMTDKDI 

        70         80         90        100        110        120 
ADKVYIEPIT LEFVTRILRK ERPDALLPTL GGQTGLNMAM ALSKNGILEE LNVELLGTKL 

       130        140        150        160        170        180 
SAIDKAEDRD LFKQLMEELN QPIPESEIVN SVEEAIQFAE QIGYPLIVRP AFTLGGTGGG 

       190        200        210        220        230        240 
MCDNQEQLVD ITTKGLKLSP VTQCLIERSI AGFKEIEYEV MRDAADNALV VCNMENFDPV 

       250        260        270        280        290        300 
GIHTGDSIVF APAQTLSDVE NQLLRDASLD IIRALKIEGG CNVQLALDPN SFKYYVIEVN 

       310        320        330        340        350        360 
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVINPITK TTYAMFEPAL DYVVAKMPRF 

       370        380        390        400        410        420 
PFDKFESGDR KLGTQMKATG EVMAIGRNIE ESLLKACRSL EIGVDHIKIA DLDNVSDDVL 

       430        440        450        460        470        480 
LEKIRKAEDD RLFYLAEALR RHYSIEKLAS LTSIDSFFLD KLRVIVELED LLSKNRLDIN 

       490        500        510        520        530        540 
ILKKVKNKGF SDKAIASLWQ INEDQVRNMR KEAGILPVYK MVDTCASEFD SATPYFYSTY 

       550        560        570        580        590        600 
AVENESLISD KASILVLGSG PIRIGQGVEF DYATVHSVKA IRESGFEAII MNSNPETVST 

       610        620        630        640        650        660 
DFSISDKLYF EPLTFEDVMN VIDLEKPEGV ILQFGGQTAI NLAKDLNKAG VKILGTQLED 

       670        680        690        700        710        720 
LDRAENRKQF EATLQALNIP QPPGFTATTE EEAVNAAQKI GYPVLVRPSY VLGGRAMKIV 

       730        740        750        760        770        780 
ENEEDLRHYM TTAVKASPDH PVLIDAYLIG KECEVDAISD GQNILIPGIM EHIERSGVHS 

       790        800        810        820        830        840 
GDSMAVYPPQ TLSETIIETI VDYTKRLAIG LNCIGMMNIQ FVIKDQKVYV IEVNPRASRT 

       850        860        870        880        890        900 
LPFLSKVTHI PMAQVATKVI LGDKLCNFTY GYDLYPASDM VHIKAPVFSF TKLAKVDSLL 

       910        920        930        940        950        960 
GPEMKSTGEV MGSDINLQKA LYKAFEAAYL HMPDYGNIVF TVDDTDKEEA LELAKVYQSI 

       970        980        990       1000       1010       1020 
GYRIYATQGT AIYFDANGLE TVLVGKLGEN DRNHIPDLIK NGKIQAVINT VGQNNIDNHD 

      1030       1040       1050       1060 
ALIIRRSAIE QGVPLFTSLD TAHAMFKVLE SRAFTLKVLD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009948 Genomic DNA. Translation: AAM99924.1.
RefSeqNP_688052.1. NC_004116.1.

3D structure databases

ProteinModelPortalQ8DZQ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208435.SAG1042.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM99924; AAM99924; SAG1042.
GeneID1013846.
KEGGsag:SAG1042.
PATRIC19628924. VBIStrAga72745_1053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSAGA208435:GHVY-1133-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 nameCARB_STRA5
AccessionPrimary (citable) accession number: Q8DZQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways