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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi286Magnesium or manganese 1UniRule annotation1
Metal bindingi300Magnesium or manganese 1UniRule annotation1
Metal bindingi300Magnesium or manganese 2UniRule annotation1
Metal bindingi302Magnesium or manganese 2UniRule annotation1
Metal bindingi837Magnesium or manganese 3UniRule annotation1
Metal bindingi849Magnesium or manganese 3UniRule annotation1
Metal bindingi849Magnesium or manganese 4UniRule annotation1
Metal bindingi851Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi160 – 217ATPUniRule annotationAdd BLAST58
Nucleotide bindingi712 – 769ATPUniRule annotationAdd BLAST58

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis
LigandATP-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 lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001450571 – 1081Carbamoyl-phosphate synthase large chainAdd BLAST1081

Proteomic databases

PaxDbiQ55756
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 interactors
STRINGi1148.SYNGTS_2440

Structurei

3D structure databases

ProteinModelPortaliQ55756
SMRiQ55756
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 329ATP-grasp 1UniRule annotationAdd BLAST197
Domaini686 – 878ATP-grasp 2UniRule annotationAdd BLAST193
Domaini945 – 1081MGS-likePROSITE-ProRule annotationAdd BLAST137

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 403Carboxyphosphate synthetic domainAdd BLAST403
Regioni404 – 553Oligomerization domainAdd BLAST150
Regioni554 – 944Carbamoyl phosphate synthetic domainAdd BLAST391
Regioni945 – 1081Allosteric domainAdd BLAST137

Sequence similaritiesi

Belongs to the CarB family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000234582
InParanoidiQ55756
KOiK01955
OMAiAVFPFNK
PhylomeDBiQ55756

Family and domain databases

CDDicd01424 MGS_CPS_II, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.40.50.1380, 1 hit
HAMAPiMF_01210_A CPSase_L_chain_A, 1 hit
MF_01210_B CPSase_L_chain_B, 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
IPR033937 MGS_CPS_CarB
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
SM00851 MGS, 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, 1 hit
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 1 hit

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 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

Entry informationi

Entry nameiCARB_SYNY3
AccessioniPrimary (citable) accession number: Q55756
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: March 28, 2018
This is version 129 of the entry and version 2 of the sequence. See 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

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