Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbamoyl-phosphate synthase small chain

Gene

carA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from bicarbonate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase catalytic chain (pyrB)
  3. Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei269NucleophileBy similarity1
Active sitei353By similarity1
Active sitei355By similarity1

GO - Molecular functioni

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: EcoliWiki
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • arginine biosynthetic process Source: EcoliWiki
  • glutamine metabolic process Source: EcoliWiki
  • urea cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CARBPSYN-SMALL.
ECOL316407:JW0030-MONOMER.
MetaCyc:CARBPSYN-SMALL.
SABIO-RKP0A6F1.
UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Protein family/group databases

MEROPSiC26.954.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase small chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase glutamine chain
Gene namesi
Name:carA
Synonyms:pyrA
Ordered Locus Names:b0032, JW0030
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10134. carA.

Subcellular locationi

GO - Cellular componenti

  • carbamoyl-phosphate synthase complex Source: EcoCyc
  • cytoplasm Source: EcoliWiki
  • cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001122741 – 382Carbamoyl-phosphate synthase small chainAdd BLAST382

Proteomic databases

EPDiP0A6F1.
PaxDbiP0A6F1.
PRIDEiP0A6F1.

2D gel databases

SWISS-2DPAGEP0A6F1.

Interactioni

Subunit structurei

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. Tetramer of heterodimers (alpha,beta)4.

Binary interactionsi

WithEntry#Exp.IntActNotes
carBP0096811EBI-546107,EBI-546118
yejGP0AD212EBI-546107,EBI-1127956

Protein-protein interaction databases

BioGridi4263445. 6 interactors.
DIPiDIP-35412N.
IntActiP0A6F1. 16 interactors.
STRINGi511145.b0032.

Chemistry databases

BindingDBiP0A6F1.

Structurei

Secondary structure

1382
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi14 – 19Combined sources6
Beta strandi23 – 33Combined sources11
Helixi39 – 43Combined sources5
Helixi46 – 48Combined sources3
Beta strandi51 – 55Combined sources5
Beta strandi57 – 59Combined sources3
Helixi67 – 69Combined sources3
Beta strandi71 – 74Combined sources4
Beta strandi77 – 81Combined sources5
Helixi98 – 104Combined sources7
Beta strandi108 – 113Combined sources6
Helixi115 – 125Combined sources11
Beta strandi128 – 137Combined sources10
Helixi140 – 149Combined sources10
Beta strandi153 – 155Combined sources3
Helixi159 – 162Combined sources4
Beta strandi168 – 170Combined sources3
Turni177 – 179Combined sources3
Helixi187 – 189Combined sources3
Beta strandi192 – 200Combined sources9
Helixi203 – 211Combined sources9
Beta strandi214 – 220Combined sources7
Helixi225 – 229Combined sources5
Beta strandi234 – 238Combined sources5
Beta strandi242 – 245Combined sources4
Helixi249 – 258Combined sources10
Turni259 – 262Combined sources4
Beta strandi265 – 268Combined sources4
Helixi270 – 278Combined sources9
Beta strandi283 – 299Combined sources17
Turni300 – 303Combined sources4
Beta strandi304 – 316Combined sources13
Helixi318 – 320Combined sources3
Beta strandi325 – 331Combined sources7
Turni332 – 334Combined sources3
Beta strandi337 – 352Combined sources16
Beta strandi357 – 359Combined sources3
Turni362 – 364Combined sources3
Helixi365 – 379Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A9XX-ray1.80B/D/F/H2-380[»]
1BXRX-ray2.10B/D/F/H1-382[»]
1C30X-ray2.00B/D/F/H1-382[»]
1C3OX-ray2.10B/D/F/H1-382[»]
1CE8X-ray2.10B/D/F/H1-380[»]
1CS0X-ray2.00B/D/F/H1-382[»]
1JDBX-ray2.10C/F/I/L1-382[»]
1KEEX-ray2.10B/D/F/H1-382[»]
1M6VX-ray2.10B/D/F/H1-382[»]
1T36X-ray2.10B/D/F/H1-382[»]
ProteinModelPortaliP0A6F1.
SMRiP0A6F1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6F1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini193 – 380Glutamine amidotransferase type-1Add BLAST188

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 189CPSaseAdd BLAST189

Sequence similaritiesi

Belongs to the CarA family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105C1M. Bacteria.
COG0505. LUCA.
HOGENOMiHOG000038087.
InParanoidiP0A6F1.
KOiK01956.
OMAiCFSVQYH.
PhylomeDBiP0A6F1.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain. 1 hit.
InterProiIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamiPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTiSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR
60 70 80 90 100
QIVTLTYPHI GNVGTNDADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS
110 120 130 140 150
YLKRHNIVAI ADIDTRKLTR LLREKGAQNG CIIAGDNPDA ALALEKARAF
160 170 180 190 200
PGLNGMDLAK EVTTAEAYSW TQGSWTLTGG LPEAKKEDEL PFHVVAYDFG
210 220 230 240 250
AKRNILRMLV DRGCRLTIVP AQTSAEDVLK MNPDGIFLSN GPGDPAPCDY
260 270 280 290 300
AITAIQKFLE TDIPVFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDV
310 320 330 340 350
EKNVVMITAQ NHGFAVDEAT LPANLRVTHK SLFDGTLQGI HRTDKPAFSF
360 370 380
QGHPEASPGP HDAAPLFDHF IELIEQYRKT AK
Length:382
Mass (Da):41,431
Last modified:July 21, 1986 - v1
Checksum:i60BC26366417443F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01597 Genomic DNA. Translation: AAA23538.1.
U00096 Genomic DNA. Translation: AAC73143.1.
AP009048 Genomic DNA. Translation: BAB96601.1.
X70017 Genomic DNA. Translation: CAA49615.1.
PIRiA01128. SYECCS.
B85484.
RefSeqiNP_414573.1. NC_000913.3.
WP_000597260.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73143; AAC73143; b0032.
BAB96601; BAB96601; BAB96601.
GeneIDi949025.
KEGGiecj:JW0030.
eco:b0032.
PATRICi32115157. VBIEscCol129921_0030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01597 Genomic DNA. Translation: AAA23538.1.
U00096 Genomic DNA. Translation: AAC73143.1.
AP009048 Genomic DNA. Translation: BAB96601.1.
X70017 Genomic DNA. Translation: CAA49615.1.
PIRiA01128. SYECCS.
B85484.
RefSeqiNP_414573.1. NC_000913.3.
WP_000597260.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A9XX-ray1.80B/D/F/H2-380[»]
1BXRX-ray2.10B/D/F/H1-382[»]
1C30X-ray2.00B/D/F/H1-382[»]
1C3OX-ray2.10B/D/F/H1-382[»]
1CE8X-ray2.10B/D/F/H1-380[»]
1CS0X-ray2.00B/D/F/H1-382[»]
1JDBX-ray2.10C/F/I/L1-382[»]
1KEEX-ray2.10B/D/F/H1-382[»]
1M6VX-ray2.10B/D/F/H1-382[»]
1T36X-ray2.10B/D/F/H1-382[»]
ProteinModelPortaliP0A6F1.
SMRiP0A6F1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263445. 6 interactors.
DIPiDIP-35412N.
IntActiP0A6F1. 16 interactors.
STRINGi511145.b0032.

Chemistry databases

BindingDBiP0A6F1.

Protein family/group databases

MEROPSiC26.954.

2D gel databases

SWISS-2DPAGEP0A6F1.

Proteomic databases

EPDiP0A6F1.
PaxDbiP0A6F1.
PRIDEiP0A6F1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73143; AAC73143; b0032.
BAB96601; BAB96601; BAB96601.
GeneIDi949025.
KEGGiecj:JW0030.
eco:b0032.
PATRICi32115157. VBIEscCol129921_0030.

Organism-specific databases

EchoBASEiEB0132.
EcoGeneiEG10134. carA.

Phylogenomic databases

eggNOGiENOG4105C1M. Bacteria.
COG0505. LUCA.
HOGENOMiHOG000038087.
InParanoidiP0A6F1.
KOiK01956.
OMAiCFSVQYH.
PhylomeDBiP0A6F1.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.
BioCyciEcoCyc:CARBPSYN-SMALL.
ECOL316407:JW0030-MONOMER.
MetaCyc:CARBPSYN-SMALL.
SABIO-RKP0A6F1.

Miscellaneous databases

EvolutionaryTraceiP0A6F1.
PROiP0A6F1.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain. 1 hit.
InterProiIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamiPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTiSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARA_ECOLI
AccessioniPrimary (citable) accession number: P0A6F1
Secondary accession number(s): P00907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.