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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Arthrobacter aurescens (strain TC1)
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 bindingi285Magnesium or manganese 1UniRule annotation1
Metal bindingi299Magnesium or manganese 1UniRule annotation1
Metal bindingi299Magnesium or manganese 2UniRule annotation1
Metal bindingi301Magnesium or manganese 2UniRule annotation1
Metal bindingi827Magnesium or manganese 3UniRule annotation1
Metal bindingi839Magnesium or manganese 3UniRule annotation1
Metal bindingi839Magnesium or manganese 4UniRule annotation1
Metal bindingi841Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi703 – 760ATPUniRule 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:AAur_2265
OrganismiArthrobacter aurescens (strain TC1)
Taxonomic identifieri290340 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaePaenarthrobacter
Proteomesi
  • UP000000637 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000663341 – 1102Carbamoyl-phosphate synthase large chainAdd BLAST1102

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

STRINGi290340.AAur_2265.

Structurei

3D structure databases

ProteinModelPortaliA1R6Z3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 328ATP-grasp 1UniRule annotationAdd BLAST196
Domaini677 – 868ATP-grasp 2UniRule annotationAdd BLAST192

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 402Carboxyphosphate synthetic domainAdd BLAST402
Regioni403 – 548Oligomerization domainAdd BLAST146
Regioni549 – 950Carbamoyl phosphate synthetic domainAdd BLAST402
Regioni951 – 1102Allosteric domainAdd BLAST152

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_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.

A1R6Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRTDLKSV LVIGSGPIVI GQAAEFDYSG TQALRVLKEE GLRVILVNSN
60 70 80 90 100
PATIMTDPEF ADATYVEPIT PEVVEKIIAK ERPDAILPTL GGQTALNTAI
110 120 130 140 150
ALDKNGVLEK YNVELIGANI AAIELGEDRE KFKGVVERCG AESARSHIIH
160 170 180 190 200
TMEEAFAAAE DLGYPMVVRP SFTMGGLGSG LAYNEDDLRR IVGQGLQYSP
210 220 230 240 250
TTEVLLEESI LGWKEYELEM MRDKNDNVVV VCSIENFDPV GVHTGDSITV
260 270 280 290 300
APALTLTDRE YQKLRDVSIA VIREVGVDTG GCNIQFAIDP ATGRVVVIEM
310 320 330 340 350
NPRVSRSSAL ASKATGFAIA KIATKLSLGY TLDEIPNDIT QKTPASFEPT
360 370 380 390 400
LDYVVVKVPR FAFEKFPAAD NTLTTTMKSV GEAMAMGRNF TEALQKALRS
410 420 430 440 450
LEQKGSQLDF SSVPEYEVAE LIEKAKRPTT DRLHQVQRAL LGGATVEDLF
460 470 480 490 500
EATKIDPWFL DQLQLLNETA QEIRKAGVLT EEMLRNAKRH GFSDEQIGAL
510 520 530 540 550
THNNEAVVRG VRQALGIRPV YKTVDTCAAE FAAYTPYHYS SYDEEDEVGL
560 570 580 590 600
HAKPSVIILG SGPNRIGQGI EFDYSCVHAS MALRKAGYET VMVNCNPETV
610 620 630 640 650
STDYDVSTRL YFEPLTLEDV LEVIAAEERT GGVMGVFVQL GGQTPLKLAQ
660 670 680 690 700
QLADAGVPIL GTSPEAIDLA EHRGAFARVL DEAGLTSPKN GTAVSFEDAK
710 720 730 740 750
KIADEIGYPV LVRPSYVLGG RGMEIVYDEA NLSRYIANAT EITPDHPVLI
760 770 780 790 800
DRFLEDAVEI DVDALFDGTD MYLGGIMEHI EEAGIHSGDS ACVLPPITLG
810 820 830 840 850
NNVIERVRTA TRAIAEGVGV RGLINIQFAL ASDVLYVLEA NPRASRTVPF
860 870 880 890 900
VSKATGVQMA KAAALIGTGV TINQLRGAYK MLPETGDGST LPLDAPVAVK
910 920 930 940 950
EAVLPFSRFR TPEGKVVDSL LGPEMRSTGE VMGIDKHFDT AFAKSQAAAN
960 970 980 990 1000
NALPTEGKIF VSVANRDKRS VIMGVKRLSD LGFEIVSTGG TADVLRRNGI
1010 1020 1030 1040 1050
QATPVRKVAE GSSAEGEGTI ADLVIAGEID MVFNTPSGGE ARSDGYELRA
1060 1070 1080 1090 1100
AATSIGIPCI TTVAEFNAAV QAIEALRTYE WSVTSLQEHA ANLSAAMEAA

NA
Length:1,102
Mass (Da):118,542
Last modified:February 6, 2007 - v1
Checksum:i5ABD714C3A92E13F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000474 Genomic DNA. Translation: ABM06627.1.
RefSeqiWP_011774949.1. NC_008711.1.

Genome annotation databases

EnsemblBacteriaiABM06627; ABM06627; AAur_2265.
KEGGiaau:AAur_2265.
PATRICi20979952. VBIArtAur67810_2300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000474 Genomic DNA. Translation: ABM06627.1.
RefSeqiWP_011774949.1. NC_008711.1.

3D structure databases

ProteinModelPortaliA1R6Z3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290340.AAur_2265.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM06627; ABM06627; AAur_2265.
KEGGiaau:AAur_2265.
PATRICi20979952. VBIArtAur67810_2300.

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_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_ARTAT
AccessioniPrimary (citable) accession number: A1R6Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: November 30, 2016
This is version 73 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, Reference 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.