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Protein

Carbamoyl-phosphate synthase arginine-specific large chain

Gene

CPA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Miscellaneous

In eukaryotes this enzyme is synthesized by two pathway-specific (arginine and pyrimidine) under separate control.
Present with 18000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 3 Mn2+ ions per subunit.By similarity

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 arginine-specific large chain (CPA2), Carbamoyl-phosphate synthase arginine-specific small chain (CPA1)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi303Manganese 1By similarity1
Metal bindingi317Manganese 1By similarity1
Metal bindingi317Manganese 2By similarity1
Metal bindingi319Manganese 2By similarity1
Metal bindingi848Manganese 3By similarity1
Metal bindingi861Manganese 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi174 – 229ATPPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi321 – 371ATPPROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YJR109C-MONOMER.
ReactomeiR-SCE-70635. Urea cycle.
UniPathwayiUPA00068; UER00171.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase arginine-specific large chain (EC:6.3.5.5)
Alternative name(s):
Arginine-specific carbamoyl-phosphate synthetase, ammonia chain
Gene namesi
Name:CPA2
Ordered Locus Names:YJR109C
ORF Names:J2002
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR109C.
SGDiS000003870. CPA2.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001450911 – 1118Carbamoyl-phosphate synthase arginine-specific large chainAdd BLAST1118

Proteomic databases

MaxQBiP03965.
PRIDEiP03965.

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.

Protein-protein interaction databases

BioGridi33865. 42 interactors.
DIPiDIP-1023N.
IntActiP03965. 34 interactors.
MINTiMINT-639311.
STRINGi4932.YJR109C.

Structurei

3D structure databases

ProteinModelPortaliP03965.
SMRiP03965.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini154 – 346ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
Domaini698 – 890ATP-grasp 2PROSITE-ProRule annotationAdd BLAST193

Sequence similaritiesi

Belongs to the CarB family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00900000141043.
HOGENOMiHOG000234583.
InParanoidiP03965.
KOiK01955.
OMAiAVFPFNK.
OrthoDBiEOG092C0957.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.40.50.1380. 1 hit.
InterProiView protein in InterPro
IPR011761. ATP-grasp.
IPR006275. CarbamoylP_synth_lsu.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR036897. CarbamoylP_synth_lsu_oligo_sf.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR036914. MGS-like_dom_sf.
IPR016185. PreATP-grasp_dom_sf.
PfamiView protein in Pfam
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF02142. MGS. 1 hit.
PRINTSiPR00098. CPSASE.
SMARTiView protein in SMART
SM01096. CPSase_L_D3. 1 hit.
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiView protein in PROSITE
PS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.

Sequencei

Sequence statusi: Complete.

P03965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSIYTSTEP TNSAFTTEDY KPQLVEGVNS VLVIGSGGLS IGQAGEFDYS
60 70 80 90 100
GSQAIKALKE DNKFTILVNP NIATNQTSHS LADKIYYLPV TPEYITYIIE
110 120 130 140 150
LERPDAILLT FGGQTGLNCG VALDESGVLA KYNVKVLGTP IKTLITSEDR
160 170 180 190 200
DLFASALKDI NIPIAESFAC ETVDEALEAA ERVKYPVIVR SAYALGGLGS
210 220 230 240 250
GFANNASEMK ELAAQSLSLA PQILVEKSLK GWKEVEYEVV RDRVGNCITV
260 270 280 290 300
CNMENFDPLG VHTGDSMVFA PSQTLSDEEF HMLRSAAIKI IRHLGVIGEC
310 320 330 340 350
NVQYALQPDG LDYRVIEVNA RLSRSSALAS KATGYPLAYT AAKIGLGYTL
360 370 380 390 400
PELPNPITKT TVANFEPSLD YIVAKIPKWD LSKFQYVDRS IGSSMKSVGE
410 420 430 440 450
VMAIGRNYEE AFQKALRQVD PSLLGFQGST EFGDQLDEAL RTPTDRRVLA
460 470 480 490 500
IGQALIHENY TVERVNELSK IDKWFLYKCM NIVNIYKELE SVKSLSDLSK
510 520 530 540 550
DLLQRAKKLG FSDKQIAVTI NKHASTNINE LEIRSLRKTL GIIPFVKRID
560 570 580 590 600
TLAAEFPAQT NYLYTTYNAT KNDVEFNENG MLVLGSGVYR IGSSVEFDWC
610 620 630 640 650
AVNTAKTLRD QGKKTIMINY NPETVSTDFD EVDRLYFEEL SYERVMDIYE
660 670 680 690 700
LEQSEGCIIS VGGQLPQNIA LKLYDNGCNI MGTNPNDIDR AENRHKFSSI
710 720 730 740 750
LDSIDVDQPE WSELTSVEEA KLFASKVNYP VLIRPSYVLS GAAMSVVNNE
760 770 780 790 800
EELKAKLTLA SDVSPDHPVV MSKFIEGAQE IDVDAVAYNG NVLVHAISEH
810 820 830 840 850
VENAGVHSGD ASLVLPPQHL SDDVKIALKD IADKVAKAWK ITGPFNMQII
860 870 880 890 900
KDGEHTLKVI ECNIRASRSF PFVSKVLGVN FIEIAVKAFL GGDIVPKPVD
910 920 930 940 950
LMLNKKYDYV ATKVPQFSFT RLAGADPFLG VEMASTGEVA SFGRDLIESY
960 970 980 990 1000
WTAIQSTMNF HVPLPPSGIL FGGDTSREYL GQVASIVATI GYRIYTTNET
1010 1020 1030 1040 1050
TKTYLQEHIK EKNAKVSLIK FPKNDKRKLR ELFQEYDIKA VFNLASKRAE
1060 1070 1080 1090 1100
STDDVDYIMR RNAIDFAIPL FNEPQTALLF AKCLKAKIAE KIKILESHDV
1110
IVPPEVRSWD EFIGFKAY
Length:1,118
Mass (Da):123,915
Last modified:October 23, 1986 - v1
Checksum:i887FAAE00AC07674
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01178 Genomic DNA. Translation: AAA66902.1.
Z49609 Genomic DNA. Translation: CAA89639.1.
BK006943 Genomic DNA. Translation: DAA08894.1.
PIRiA01199. SYBYCP.
RefSeqiNP_012643.3. NM_001181767.3.

Genome annotation databases

EnsemblFungiiYJR109C; YJR109C; YJR109C.
GeneIDi853573.
KEGGisce:YJR109C.

Similar proteinsi

Entry informationi

Entry nameiCARB_YEAST
AccessioniPrimary (citable) accession number: P03965
Secondary accession number(s): D6VWS8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: November 22, 2017
This is version 183 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names