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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 4 Mg2+ or 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.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
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.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
  2. Aspartate carbamoyltransferase (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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi286 – 2861Magnesium or manganese 1UniRule annotation
Metal bindingi300 – 3001Magnesium or manganese 1UniRule annotation
Metal bindingi300 – 3001Magnesium or manganese 2UniRule annotation
Metal bindingi302 – 3021Magnesium or manganese 2UniRule annotation
Metal bindingi837 – 8371Magnesium or manganese 3UniRule annotation
Metal bindingi849 – 8491Magnesium or manganese 3UniRule annotation
Metal bindingi849 – 8491Magnesium or manganese 4UniRule annotation
Metal bindingi851 – 8511Magnesium or manganese 4UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi160 – 21758ATPUniRule annotationAdd
BLAST
Nucleotide bindingi712 – 76958ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase large chainUniRule annotation (EC:6.3.5.5UniRule annotation)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chainUniRule annotation
Gene namesi
Name:carBUniRule annotation
Ordered Locus Names:sll0370
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10811081Carbamoyl-phosphate synthase large chainPRO_0000145057Add
BLAST

Proteomic databases

PRIDEiQ55756.

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.UniRule annotation

Protein-protein interaction databases

IntActiQ55756. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ55756.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 329197ATP-grasp 1UniRule annotationAdd
BLAST
Domaini686 – 878193ATP-grasp 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 403403Carboxyphosphate synthetic domainAdd
BLAST
Regioni404 – 553150Oligomerization domainAdd
BLAST
Regioni554 – 944391Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni945 – 1081137Allosteric domainAdd
BLAST

Sequence similaritiesi

Belongs to the CarB family.UniRule annotation
Contains 2 ATP-grasp domains.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000234582.
InParanoidiQ55756.
KOiK01955.
OMAiAVFPFNK.
PhylomeDBiQ55756.

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.
HAMAPiMF_01210_A. CPSase_L_chain_A.
MF_01210_B. CPSase_L_chain_B.
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.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 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. 1 hit.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q55756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRRNDLNKI MILGAGPIVI GQACEFDYSG TQACKALKEE GYEVVLVNSN
60 70 80 90 100
PASIMTDPEL ADRTYIEPLI PEIVEKIIEK ERPDAVLPTM GGQTALNLAV
110 120 130 140 150
SLSKSGVLEK YGVELIGAKL PAIEMGEDRE LFKEAMARIG VPVCPSGIAS
160 170 180 190 200
SIEEARQVAH EIGSYPLIIR PAFTLAGTGG GIAYNQEEYE EMVQYGLDQS
210 220 230 240 250
PMSQILVEKS LLGWKEYELE VMRDLADNVV IICSIENFDP MGVHTGDSIT
260 270 280 290 300
VAPAQTLTDK EYQRLRDYSI AIIREIGVET GGSNIQFSVN PANGDVIVIE
310 320 330 340 350
MNPRVSRSSA LASKATGFPI AKFAAKLAVG YTLNEISNDI TKKTPASFEP
360 370 380 390 400
TIDYVVTKIP RFAFEKFPGA EPILNTQMKS VGEAMAIGRT FQESFQKALR
410 420 430 440 450
SLETGRFGFG CDRHETLPTL SHLRSQLRTP NPERVFSLHH AFNLGMTVEE
460 470 480 490 500
IHELTAIDPW FLDKLEDLVK TEKYMKQRSL KDLTAADLRY IKQQGFGDRQ
510 520 530 540 550
IAFATKTTED EVRAYRKSLG ITPVYKVVDT CAAEFEAFTP YYYSTYEPEE
560 570 580 590 600
CEVLPSDKPK VMILGGGPNR IGQGIEFDYC CCHAAFSLSD AGYETIMVNS
610 620 630 640 650
NPETVSTDYD TSDRLYFEPL TKEDVLNIIE AENPVGIIIQ FGGQTPLKLA
660 670 680 690 700
VPLQKYLNSP DCPVQTKIWG TSPDSIDTAE DRERFEKILH ELEISQPPNG
710 720 730 740 750
IARDYEESRV VANRISYPVV VRPSYVLGGR AMEIVYSDEE LERYMTYAVQ
760 770 780 790 800
IEPDHPILID KFLENAIEVD VDSLTDSTGK VVIGSIMEHI EEAGIHSGDS
810 820 830 840 850
ACSIPYTSLS DNVLTTIRQW TEQLARALNV VGLMNIQYAV QGDQVYILEA
860 870 880 890 900
NPRASRTVPY VSKATGRPLA KIASLVMSGK TLEELGVTEE FIPQHVAVKE
910 920 930 940 950
AVLPFSKFPG ADTLLGPEMR STGEVMGIDS DFGKAFAKAE LGAGVILATT
960 970 980 990 1000
GTVFVSMSDR TKEAAVPVVR ELIDLGFKVV ATSGTQKVLR EHGIEGVEVV
1010 1020 1030 1040 1050
LKLHEGRPHV IDWIKNGQIQ FIINTPSGEE SQLDGRTIRR AALDYKLPII
1060 1070 1080
TTIAGGKATV AALRSLQDHP LDVKALQDYL G
Length:1,081
Mass (Da):119,031
Last modified:August 2, 2002 - v2
Checksum:i0C2E0D3905B40EE6
GO

Sequence cautioni

The sequence BAA10403.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10403.1. Different initiation.
PIRiS76557.

Genome annotation databases

EnsemblBacteriaiBAA10403; BAA10403; BAA10403.
KEGGisyn:sll0370.
PATRICi23842338. VBISynSp132158_2709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10403.1. Different initiation.
PIRiS76557.

3D structure databases

ProteinModelPortaliQ55756.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ55756. 2 interactions.

Proteomic databases

PRIDEiQ55756.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10403; BAA10403; BAA10403.
KEGGisyn:sll0370.
PATRICi23842338. VBISynSp132158_2709.

Phylogenomic databases

HOGENOMiHOG000234582.
InParanoidiQ55756.
KOiK01955.
OMAiAVFPFNK.
PhylomeDBiQ55756.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

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.
HAMAPiMF_01210_A. CPSase_L_chain_A.
MF_01210_B. CPSase_L_chain_B.
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.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 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. 1 hit.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiCARB_SYNY3
AccessioniPrimary (citable) accession number: Q55756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: March 16, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.