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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Status
Reviewed-Annotation score: Annotation score: 3 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)DescriptionActionsGraphical viewLength
Metal bindingi284Magnesium or manganese 1UniRule annotation1
Metal bindingi298Magnesium or manganese 1UniRule annotation1
Metal bindingi298Magnesium or manganese 2UniRule annotation1
Metal bindingi300Magnesium or manganese 2UniRule annotation1
Metal bindingi820Magnesium or manganese 3UniRule annotation1
Metal bindingi832Magnesium or manganese 3UniRule annotation1
Metal bindingi832Magnesium or manganese 4UniRule annotation1
Metal bindingi834Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi697 – 754ATPUniRule annotationAdd BLAST58

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:lwe1854
OrganismiListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Taxonomic identifieri386043 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000000779 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000663611 – 1070Carbamoyl-phosphate synthase large chainAdd BLAST1070

Proteomic databases

PRIDEiA0AJU0.

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

STRINGi386043.lwe1854.

Structurei

3D structure databases

ProteinModelPortaliA0AJU0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 327ATP-grasp 1UniRule annotationAdd BLAST195
Domaini671 – 861ATP-grasp 2UniRule annotationAdd BLAST191

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 401Carboxyphosphate synthetic domainAdd BLAST401
Regioni402 – 546Oligomerization domainAdd BLAST145
Regioni547 – 929Carbamoyl phosphate synthetic domainAdd BLAST383
Regioni930 – 1070Allosteric domainAdd BLAST141

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.
OMAiSTAYMYS.
OrthoDBiPOG091H01IP.

Family and domain databases

CDDicd01424. MGS_CPS_II. 1 hit.
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.
IPR033937. MGS_CPS_CarB.
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.

A0AJU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRDDIKTI LVIGSGPIVI GQAAEFDYAG TQACLSLKEE GYRVVLVNSN
60 70 80 90 100
PATIMTDAEM ADKVYIEPIT LDFVSRIIRK ERPDAILPTL GGQTGLNMAM
110 120 130 140 150
ELSAAGILDE CNVEVLGTDL TAIKKAEDRE AFRDLMNELG EPVPESDIIH
160 170 180 190 200
NLDEAYSFVE RIGYPVIVRP AYTLGGSGGG ICHNEQELIE TVTSGLKLSP
210 220 230 240 250
VTQCLLEKSI AGFKEVEYEV MRDANNNAMV VCNMENIDPV GIHTGDSIVV
260 270 280 290 300
APSQTLSDRE YQLLRDVSLK IIRALEIEGG CNVQLALDPD SYNYYVIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVRNPVTG TTFAHFEPTL
360 370 380 390 400
DYVVAKIPRF AFDKFEQADR RLGTQMKATG EVMAIGRSWE EALLKAVRSL
410 420 430 440 450
EVGADHLLLE EAENADEETL ERKICFPEDD RLFFLAAALR RGQTIEQLHE
460 470 480 490 500
KTKIDLFFLY KLSKSIELEN RVKENPQNEA ILAEAKRAGF SDAFLATCWN
510 520 530 540 550
IDEQAIYDLR KAQNLFPVYK MVDTCAAEFE STTPYFYSTY EEENESTRSA
560 570 580 590 600
KESVIVLGSG PIRIGQGVEF DYATVHSVWA IQQAGYEAII INNNPETVST
610 620 630 640 650
DFSISDKLYF EPLTLEDVMH VIEIEQPLGV VVQFGGQTAI NLADGLAKRG
660 670 680 690 700
VKILGTSLED TDRAENRDAF EKALEILQIP QPAGKTATSV EEAIKVATDI
710 720 730 740 750
GYPVLVRPSY VLGGRAMEIV ESEEALKHYM TNAVKVNPKH PVLVDRYVSG
760 770 780 790 800
QEVEVDAISD GENVLIPGIM EHIERAGVHS GDSIAVYPAQ RLSQQVKNTI
810 820 830 840 850
VDYTTRLATG LNIIGMLNIQ YVVDGEEVFV IEVNPRSSRT APFLSKITEI
860 870 880 890 900
PMANVATRVI LGENLIDLGY TPGLAPEKQE IFVKVPVFSF AKLRSVDTSL
910 920 930 940 950
GPEMKSTGEV MGKDVTLEKA LYKGFVASGT TMHDYGTVLL TVADRDKKEA
960 970 980 990 1000
VELAKRFNRI GFTIMATKGT ASTLEEAEIP VSQVKKIGEN QETLIDYIRN
1010 1020 1030 1040 1050
GQVTLVVNTL TTGKRPERDG FQIRRESVEN GIPVCTSLDT AEAILRVLES
1060 1070
RSFELESMNA SEVKQPKVRV
Length:1,070
Mass (Da):117,917
Last modified:November 28, 2006 - v1
Checksum:i80EF88E233B18DE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM263198 Genomic DNA. Translation: CAK21272.1.
RefSeqiWP_011702624.1. NC_008555.1.

Genome annotation databases

EnsemblBacteriaiCAK21272; CAK21272; lwe1854.
KEGGilwe:lwe1854.
PATRICi20330913. VBILisWel39304_1863.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM263198 Genomic DNA. Translation: CAK21272.1.
RefSeqiWP_011702624.1. NC_008555.1.

3D structure databases

ProteinModelPortaliA0AJU0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi386043.lwe1854.

Proteomic databases

PRIDEiA0AJU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAK21272; CAK21272; lwe1854.
KEGGilwe:lwe1854.
PATRICi20330913. VBILisWel39304_1863.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
KOiK01955.
OMAiSTAYMYS.
OrthoDBiPOG091H01IP.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Family and domain databases

CDDicd01424. MGS_CPS_II. 1 hit.
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.
IPR033937. MGS_CPS_CarB.
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_LISW6
AccessioniPrimary (citable) accession number: A0AJU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 28, 2006
Last modified: November 30, 2016
This is version 75 of the entry and version 1 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.