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 arginine-specific large chain

Gene

arg4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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 (arg4), Carbamoyl-phosphate synthase arginine-specific small chain (arg5)
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 bindingi361Manganese 1By similarity1
Metal bindingi375Manganese 1By similarity1
Metal bindingi375Manganese 2By similarity1
Metal bindingi377Manganese 2By similarity1
Metal bindingi898Manganese 3By similarity1
Metal bindingi917Manganese 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi232 – 287ATPPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi379 – 429ATPPROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-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:arg4
ORF Names:SPBC215.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC215.08c.
PomBaseiSPBC215.08c. arg4.

Subcellular locationi

GO - Cellular componenti

  • carbamoyl-phosphate synthase complex Source: PomBase
  • cytoplasm Source: GO_Central
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001450891 – 1160Carbamoyl-phosphate synthase arginine-specific large chainAdd BLAST1160

Proteomic databases

MaxQBiO94313.
PRIDEiO94313.

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.By similarity

Protein-protein interaction databases

BioGridi277252. 2 interactors.
DIPiDIP-59124N.
MINTiMINT-4683120.

Structurei

3D structure databases

ProteinModelPortaliO94313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini212 – 404ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
Domaini748 – 946ATP-grasp 2PROSITE-ProRule annotationAdd BLAST199

Sequence similaritiesi

Belongs to the CarB family.Curated
Contains 2 ATP-grasp domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000234583.
InParanoidiO94313.
KOiK01955.
OMAiSTAYMYS.
OrthoDBiEOG092C0957.
PhylomeDBiO94313.

Family and domain databases

Gene3Di1.10.1030.10. 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.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
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]
PfamiPF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALWATSMRR AIPGISKAFL GSNRVLETAG VSQLSKHLLP QWSGVPHRKI
60 70 80 90 100
SASATNFNDK VKESNTPDAN AYIRSGHIKA AEHEKVKKVV VVGSGGLSIG
110 120 130 140 150
QAGEFDYSGA QAIKALRESS VHTILINPNI ATIQSSHSLA DEIYFLPVTA
160 170 180 190 200
EYLTHLIERE NPDGILLTFG GQTALNVGIQ LDDMGVFARN HVKVLGTPIS
210 220 230 240 250
TLKTSEDRDL FAKALNEINI PIAESVAVST VDEALQAAEK VSYPVIIRSA
260 270 280 290 300
YSLGGLGSGF ANNKEELQSM AAKSLSLTPQ ILVEKSLKGW KEVEYEVVRD
310 320 330 340 350
AANNCITVCN MENFDPLGIH TGDSIVVAPS QTLSDEEYHM LRTAAIKIIR
360 370 380 390 400
HLGVVGECNV QYALSPNSLE YRVIEVNARL SRSSALASKA TGYPLAYTAA
410 420 430 440 450
KIALGHTLPE LPNAVTKTTT ANFEPSLDYV VTKIPRWDLS KFQYVNREIG
460 470 480 490 500
SSMKSVGEVM AVGRTFEESL QKALRQVDPS FLGFMAMPFK DLDNALSVPT
510 520 530 540 550
DRRFFAVVEA MLNQGYSIDK IHDLTKIDKW FLSKLANMAK VYKELEEIGS
560 570 580 590 600
LYGLNKEIML RAKKTGFSDL QISKLVGASE LDVRARRKRL DVHPWVKKID
610 620 630 640 650
TLAAEFPAHT NYLYTSYNAS SHDIDFNEHG TMVLGSGVYR IGSSVEFDWC
660 670 680 690 700
GVSCARTLRK LGHSTIMVNY NPETVSTDFD ECERLYFEEL SYERVMDIYE
710 720 730 740 750
METASGIVVS VGGQLPQNIA LKLQETGAKV LGTDPLMIDS AEDRHKFSQI
760 770 780 790 800
LDKIGVDQPA WKELTSVAEA SKFANAVGYP VLVRPSYVLS GAAMSVIRDE
810 820 830 840 850
SSLKDKLENA SAVSPDHPVV ITKFIEGARE LDVDAVASKG KLLVHAVSEH
860 870 880 890 900
VENAGVHSGD ATIALPPYSL SEDILSRCKE IAEKVCKAFQ ITGPYNMQII
910 920 930 940 950
LAQNPDKPDT PDLKVIECNL RASRSFPFVS KTLGVNFIDV ATRSIIDQEV
960 970 980 990 1000
PAARDLMAVH RDYVCVKVPQ FSWTRLAGAD PYLGVEMSST GEVACFGKDV
1010 1020 1030 1040 1050
KEAYWAALQS TQNFKIPLPG QGILLGGDRP ELAGIAADLS KLGYKLYVAN
1060 1070 1080 1090 1100
KDAAKLLQPT SAEVVEFPVK DKRALRAIFE KYNIRSVFNL ASARGKNVLD
1110 1120 1130 1140 1150
QDYVMRRNAV DFNVTLINDV NCAKLFVESL KEKLPSVLSE KKEMPSEVKR
1160
WSEWIGSHDL
Length:1,160
Mass (Da):127,480
Last modified:May 1, 1999 - v1
Checksum:i883FBAC4A8E79BC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22122.1.
PIRiT39898.
RefSeqiNP_596685.1. NM_001022608.2.

Genome annotation databases

EnsemblFungiiSPBC215.08c.1; SPBC215.08c.1:pep; SPBC215.08c.
GeneIDi2540729.
KEGGispo:SPBC215.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22122.1.
PIRiT39898.
RefSeqiNP_596685.1. NM_001022608.2.

3D structure databases

ProteinModelPortaliO94313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277252. 2 interactors.
DIPiDIP-59124N.
MINTiMINT-4683120.

Proteomic databases

MaxQBiO94313.
PRIDEiO94313.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC215.08c.1; SPBC215.08c.1:pep; SPBC215.08c.
GeneIDi2540729.
KEGGispo:SPBC215.08c.

Organism-specific databases

EuPathDBiFungiDB:SPBC215.08c.
PomBaseiSPBC215.08c. arg4.

Phylogenomic databases

HOGENOMiHOG000234583.
InParanoidiO94313.
KOiK01955.
OMAiSTAYMYS.
OrthoDBiEOG092C0957.
PhylomeDBiO94313.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
ReactomeiR-SPO-70635. Urea cycle.

Miscellaneous databases

PROiO94313.

Family and domain databases

Gene3Di1.10.1030.10. 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.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
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]
PfamiPF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARB_SCHPO
AccessioniPrimary (citable) accession number: O94313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes this enzyme is synthesized by two pathway-specific (arginine and pyrimidine) under separate control.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.