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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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 large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
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 large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  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 bindingi284 – 2841Magnesium or manganese 1UniRule annotation
Metal bindingi298 – 2981Magnesium or manganese 1UniRule annotation
Metal bindingi298 – 2981Magnesium or manganese 2UniRule annotation
Metal bindingi300 – 3001Magnesium or manganese 2UniRule annotation
Metal bindingi820 – 8201Magnesium or manganese 3UniRule annotation
Metal bindingi832 – 8321Magnesium or manganese 3UniRule annotation
Metal bindingi832 – 8321Magnesium or manganese 4UniRule annotation
Metal bindingi834 – 8341Magnesium or manganese 4UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPUniRule annotationAdd
BLAST
Nucleotide bindingi697 – 75458ATPUniRule 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

BioCyciLLAC416870:GCDT-1115-MONOMER.
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:llmg_1089
OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic identifieri416870 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
Proteomesi
  • UP000000364 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10641064Carbamoyl-phosphate synthase large chainPRO_0000145013Add
BLAST

Expressioni

Inductioni

Repressed by pyrimidines.

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

STRINGi416870.llmg_1089.

Structurei

3D structure databases

ProteinModelPortaliO32771.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 327195ATP-grasp 1UniRule annotationAdd
BLAST
Domaini671 – 861191ATP-grasp 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 401401Carboxyphosphate synthetic domainAdd
BLAST
Regioni402 – 546145Oligomerization domainAdd
BLAST
Regioni547 – 929383Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni930 – 1064135Allosteric domainAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
KOiK01955.
OMAiMPWSRFR.

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. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
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. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O32771-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRNDIKKI MIIGSGPIII GQAAEFDYAG TQACLALKEE GYEVVLVNSN
60 70 80 90 100
PATIMTDREI ADTVYIEPIT LEFVSKILRK ERPDALLPTL GGQTGLNMAM
110 120 130 140 150
ELSKTGILEE LNVELLGTKL SAIDQAEDRE LFKELCESIN EPLCASDIAT
160 170 180 190 200
TVEEAINIAD KIGYPIIVRP AFTMGGTGGG ICDTEEELRE IVANGLKLSP
210 220 230 240 250
VTQCLIEESI AGYKEIEYEV MRDSADNAIV VCNMENFDPV GVHTGDSIVF
260 270 280 290 300
APSQTLSDNE YQMLRDASLN IIRALKIEGG CNVQLALDPN SYEYRVIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK MSAKIAIGMT LDEIINPVTN KTYAMFEPAL
360 370 380 390 400
DYVVAKIARF PFDKFENGDR HLGTQMKATG EVMAIGRNIE ESLLKAVRSL
410 420 430 440 450
EIGVFHNEMT EAIEADDEKL YEKMVKTQDD RLFYVSEAIR RGIPIEEIAD
460 470 480 490 500
LTKIDIFFLD KLLYIVEIEN QLKVNIFEPE LLKTAKKNGF SDREIAKLWN
510 520 530 540 550
VTPEEVRRRR QENKIIPVYK MVDTCAAEFE SSTPYFYSTY EWENESKRSD
560 570 580 590 600
KEKIIVLGSG PIRIGQGVEF DYATVHCVKA IQALGKEAIV INSNPETVST
610 620 630 640 650
DFSISDKLYF EPLTFEDVMN VIDLEEPLGV IVQFGGQTAI NLAEPLSKAG
660 670 680 690 700
VKILGTQVED LDRAEDRDLF EKALQDLDIP QPPGATATNE EEAVANANKI
710 720 730 740 750
GYPVLIRPSF VLGGRAMEII NNEKDLRDYM NRAVKASPEH PVLVDSYLQG
760 770 780 790 800
QECEVDAICD GKEVLLPGIM EHIERAGVHS GDSMAVYPPQ NLSQAIIDTI
810 820 830 840 850
VDYTKRLAIG LNCIGMMNIQ FVIYEEQVYV IEVNPRASRT VPFLSKVTNI
860 870 880 890 900
PMAQLATQMI LGENLKDLGY EAGLAPTPDM VHVKAPVFSF TKLAKVDSLL
910 920 930 940 950
GPEMKSTGEA MGSDVTLEKA LYKSFEAAKL HMADYGSVLF TVADEDKEET
960 970 980 990 1000
LALAKDFAEI GYSLVATAGT AAFLKENGLY VREVEKLAGG EDEEGTLVED
1010 1020 1030 1040 1050
IRQGRVQAVV NTMGNTRASL TTATDGFRIR QEAISRGIPL FTSLDTVAAI
1060
LKVMQSRSFT TKNI
Length:1,064
Mass (Da):117,429
Last modified:May 1, 2007 - v2
Checksum:iEEBB4A4CA0DBDAB5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321Q → E in CAA03928 (PubMed:9721272).Curated
Sequence conflicti169 – 1691R → G in CAA03928 (PubMed:9721272).Curated
Sequence conflicti629 – 6291G → V in CAA03928 (PubMed:9721272).Curated
Sequence conflicti645 – 6451P → H in CAA03928 (PubMed:9721272).Curated
Sequence conflicti909 – 9091E → L in CAA03928 (PubMed:9721272).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000109 Genomic DNA. Translation: CAA03928.1.
AM406671 Genomic DNA. Translation: CAL97683.1.
RefSeqiWP_011834997.1. NC_009004.1.

Genome annotation databases

EnsemblBacteriaiCAL97683; CAL97683; llmg_1089.
KEGGillm:llmg_1089.
PATRICi22283326. VBILacLac4574_1120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ000109 Genomic DNA. Translation: CAA03928.1.
AM406671 Genomic DNA. Translation: CAL97683.1.
RefSeqiWP_011834997.1. NC_009004.1.

3D structure databases

ProteinModelPortaliO32771.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_1089.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL97683; CAL97683; llmg_1089.
KEGGillm:llmg_1089.
PATRICi22283326. VBILacLac4574_1120.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
KOiK01955.
OMAiMPWSRFR.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.
BioCyciLLAC416870:GCDT-1115-MONOMER.

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. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
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. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARB_LACLM
AccessioniPrimary (citable) accession number: O32771
Secondary accession number(s): A2RK73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: May 1, 2007
Last modified: September 7, 2016
This is version 111 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.