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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Arthrobacter sp. (strain FB24)
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 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 bindingi285 – 2851Magnesium or manganese 1UniRule annotation
Metal bindingi299 – 2991Magnesium or manganese 1UniRule annotation
Metal bindingi299 – 2991Magnesium or manganese 2UniRule annotation
Metal bindingi301 – 3011Magnesium or manganese 2UniRule annotation
Metal bindingi827 – 8271Magnesium or manganese 3UniRule annotation
Metal bindingi839 – 8391Magnesium or manganese 3UniRule annotation
Metal bindingi839 – 8391Magnesium or manganese 4UniRule annotation
Metal bindingi841 – 8411Magnesium or manganese 4UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPUniRule annotationAdd
BLAST
Nucleotide bindingi703 – 76058ATPUniRule 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

BioCyciASP290399:GHIF-2308-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:Arth_2262
OrganismiArthrobacter sp. (strain FB24)
Taxonomic identifieri290399 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter
Proteomesi
  • UP000000754 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10991099Carbamoyl-phosphate synthase large chainPRO_1000066335Add
BLAST

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

STRINGi290399.Arth_2262.

Structurei

3D structure databases

ProteinModelPortaliA0JX72.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 328196ATP-grasp 1UniRule annotationAdd
BLAST
Domaini677 – 868192ATP-grasp 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 402402Carboxyphosphate synthetic domainAdd
BLAST
Regioni403 – 548146Oligomerization domainAdd
BLAST
Regioni549 – 950402Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni951 – 1099149Allosteric 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.
OMAiAVFPFNK.
OrthoDBiEOG6J1DC6.

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_B. CPSase_L_chain_B.
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.

A0JX72-1 [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
SMDEALKAAE DLGYPMVVRP SFTMGGLGSG LAYTEDDLRR IVGQGLQYSP
210 220 230 240 250
TSEVLLEESI LGWKEYELEM MRDKNDNVVV VCSIENFDPV GVHTGDSITV
260 270 280 290 300
APALTLTDRE YQRLRDISIA VIREVGVDTG GCNIQFAVEP DTGRVVVIEM
310 320 330 340 350
NPRVSRSSAL ASKATGFAIA KIATKLSLGY TLDEIPNDIT QKTPASFEPT
360 370 380 390 400
LDYVVVKVPR FAFEKFPAAD PTLTTTMKSV GEAMAMGRNF TEALQKALRS
410 420 430 440 450
LEQKGSQLDF SHVPEWEVPE LIEKAKRPTT ERLHQVQRAL LGGATVEQLF
460 470 480 490 500
EATKIDPWYL DQLQLLNEIS HEIRKSTALT PEMLQRAKRH GFSDEQIGAL
510 520 530 540 550
TNNQEAVVRG VRQALGIRPV YKTVDTCAAE FAAYTPYHYS SYDEEDEVAL
560 570 580 590 600
HSKPSIIILG SGPNRIGQGI EFDYSCVHAS MALRKAGYET VMVNCNPETV
610 620 630 640 650
STDYDVSTRL YFEPLTLEDV LEVIAAEERT GGVMGVFVQL GGQTPLKLAQ
660 670 680 690 700
QLADAGVPIL GTSPEAIDLA EHRGAFSRVL DEAGLISPKN GTAVSFEDAK
710 720 730 740 750
KIADEIGYPV LVRPSYVLGG RGMEIVYDEP NLSRYIANAT EITTEHPVLI
760 770 780 790 800
DRFLEDAVEI DVDALYDGTE MYLGGIMEHI EEAGIHSGDS ACVLPPITLG
810 820 830 840 850
NNVIERVRTA TLAIAEGVGV RGLINIQFAL ASDVLYVLEA NPRASRTVPF
860 870 880 890 900
VSKATGVQMA KAAALIGTGV TINQLRSAYK MLPETGDGST LPFDAPVSVK
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 ADLIVAGEID MVFNTPSGGE ARIDGYELRA
1060 1070 1080 1090
AATSIGIPCI TTVAEFNAAV QAIEAQRTYE WSVTSLQEHA ENLKALQNG
Length:1,099
Mass (Da):118,840
Last modified:December 12, 2006 - v1
Checksum:i7BC99C4327E35E57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000454 Genomic DNA. Translation: ABK03642.1.
RefSeqiWP_011692106.1. NC_008541.1.

Genome annotation databases

EnsemblBacteriaiABK03642; ABK03642; Arth_2262.
KEGGiart:Arth_2262.
PATRICi20999867. VBIArtSp72239_2631.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000454 Genomic DNA. Translation: ABK03642.1.
RefSeqiWP_011692106.1. NC_008541.1.

3D structure databases

ProteinModelPortaliA0JX72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290399.Arth_2262.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK03642; ABK03642; Arth_2262.
KEGGiart:Arth_2262.
PATRICi20999867. VBIArtSp72239_2631.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
KOiK01955.
OMAiAVFPFNK.
OrthoDBiEOG6J1DC6.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.
BioCyciASP290399:GHIF-2308-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_B. CPSase_L_chain_B.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FB24.

Entry informationi

Entry nameiCARB_ARTS2
AccessioniPrimary (citable) accession number: A0JX72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: November 11, 2015
This is version 70 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.