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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

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

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.
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.
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 catalytic subunit (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 bindingi285Magnesium or manganese 1By similarity1
Metal bindingi299Magnesium or manganese 1By similarity1
Metal bindingi299Magnesium or manganese 2By similarity1
Metal bindingi301Magnesium or manganese 2By similarity1
Metal bindingi829Magnesium or manganese 3By similarity1
Metal bindingi841Magnesium or manganese 3By similarity1
Metal bindingi841Magnesium or manganese 4By similarity1
Metal bindingi843Magnesium or manganese 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPBy similarityAdd BLAST58
Nucleotide bindingi705 – 762ATPBy similarityAdd 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

BioCyciSENT99287:G1FZD-68-MONOMER
UniPathwayiUPA00068; UER00171
UPA00070; UER00115

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase large chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:carB
Ordered Locus Names:STM0067
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001450352 – 1075Carbamoyl-phosphate synthase large chainAdd BLAST1074

Proteomic databases

PaxDbiP14846
PRIDEiP14846

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

STRINGi99287.STM0067

Structurei

3D structure databases

ProteinModelPortaliP14846
SMRiP14846
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 328ATP-grasp 1Add BLAST196
Domaini679 – 870ATP-grasp 2Add BLAST192
Domaini937 – 1075MGS-likePROSITE-ProRule annotationAdd BLAST139

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 403Carboxyphosphate synthetic domainAdd BLAST402
Regioni404 – 553Oligomerization domainAdd BLAST150
Regioni554 – 936Carbamoyl phosphate synthetic domainAdd BLAST383
Regioni937 – 1075Allosteric domainAdd BLAST139

Sequence similaritiesi

Belongs to the CarB family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
HOGENOMiHOG000234582
KOiK01955
OMAiAVFPFNK
PhylomeDBiP14846

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, 2 hits
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14846-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN
60 70 80 90 100
PATIMTDPEM ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL
110 120 130 140 150
ELERQGVLEE FGVTMIGATA DAIDKAEDRR RFDIAMKKIG LDTARSGIAH
160 170 180 190 200
TMEEALAVAA DVGFPCIIRP SFTMGGTGGG IAYNREEFEE ICERGLDLSP
210 220 230 240 250
TNELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM GIHTGDSITV
260 270 280 290 300
APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
310 320 330 340 350
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP
360 370 380 390 400
SIDYVVTKIP RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR
410 420 430 440 450
GLEVGATGFD PKVSLDDPEA LTKIRRELKD AGADRIWYIA DAFRAGLSVD
460 470 480 490 500
GVFNLTNIDR WFLVQIEELV RLEEKVAEVG ITGLNADFLR QLKRKGFADA
510 520 530 540 550
RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT AYMYSTYEDE
560 570 580 590 600
CEANPSIDRD KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
610 620 630 640 650
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL
660 670 680 690 700
ARALEAAGVP VIGTSPDAID RAEDRERFQH AVDRLKLKQP ANATVTAIEQ
710 720 730 740 750
AVEKAKEIGY PLVVRPSYVL GGRAMEIVYD EADLRRYFQT AVSVSNDAPV
760 770 780 790 800
LLDRFLDDAV EVDVDAICDG EMVLIGGIME HIEQAGVHSG DSACSLPAYT
810 820 830 840 850
LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKDNEVYLI EVNPRAARTV
860 870 880 890 900
PFVSKATGVP LAKVAARVMA GKSLTEQGVT QEIIPPYYSV KEVVLPFNKF
910 920 930 940 950
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KQGRALLSVR
960 970 980 990 1000
EGDKERVVDL AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH
1010 1020 1030 1040 1050
IQDRIKNGEY TYIINTTAGR RAIEDSRVIR RSALQYKVHY DTTLNGGFAT
1060 1070
TMALNADATE KVTSVQEMHA QIKKS
Length:1,075
Mass (Da):118,139
Last modified:January 23, 2007 - v4
Checksum:i918D74FADFF8CC7C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti123I → G in AAB39256 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81260 Genomic DNA Translation: AAB39256.1
AE006468 Genomic DNA Translation: AAL19031.1
M36540 Genomic DNA Translation: AAA27033.1
RefSeqiNP_459072.1, NC_003197.2
WP_001126305.1, NC_003197.2

Genome annotation databases

EnsemblBacteriaiAAL19031; AAL19031; STM0067
GeneIDi1251585
KEGGistm:STM0067
PATRICifig|99287.12.peg.69

Similar proteinsi

Entry informationi

Entry nameiCARB_SALTY
AccessioniPrimary (citable) accession number: P14846
Secondary accession number(s): P96067
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 142 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health