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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi290 – 2901Magnesium or manganese 1UniRule annotation
Metal bindingi304 – 3041Magnesium or manganese 1UniRule annotation
Metal bindingi304 – 3041Magnesium or manganese 2UniRule annotation
Metal bindingi306 – 3061Magnesium or manganese 2UniRule annotation
Metal bindingi843 – 8431Magnesium or manganese 3UniRule annotation
Metal bindingi855 – 8551Magnesium or manganese 3UniRule annotation
Metal bindingi855 – 8551Magnesium or manganese 4UniRule annotation
Metal bindingi857 – 8571Magnesium or manganese 4UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 22158ATPUniRule annotationAdd
BLAST
Nucleotide bindingi719 – 77658ATPUniRule 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

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:ML0536
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0536.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11211121Carbamoyl-phosphate synthase large chainPRO_0000145022Add
BLAST

Proteomic databases

PRIDEiQ9CCR2.

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

STRINGi272631.ML0536.

Structurei

3D structure databases

ProteinModelPortaliQ9CCR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 333196ATP-grasp 1UniRule annotationAdd
BLAST
Domaini693 – 884192ATP-grasp 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 407407Carboxyphosphate synthetic domainAdd
BLAST
Regioni408 – 559152Oligomerization domainAdd
BLAST
Regioni560 – 965406Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni966 – 1121156Allosteric 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.
OrthoDBiPOG091H01IP.

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

Sequencei

Sequence statusi: Complete.

Q9CCR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRRTDLNHV LVIGSGPIVI GQACEFDYAG TQACRVLRAE GLQVSLVNSN
60 70 80 90 100
PATIMTDPEF ADHTYVEPIT PAFVERVIVQ QAERGNRIDA LLATLGGQTA
110 120 130 140 150
LNTAVALYEN GVLERYGVEL IGADFEAIQR GEDRQRFKDL VAKVGGESAR
160 170 180 190 200
SKVCFTMDEV RETVEDLGLP VVVRPSFTMG GLGSGMAHSD EEVGRMAGAG
210 220 230 240 250
LVASPSANVL IEESVYGWKE FELELMRDGH DSVVVVCSIE NVDPMGVHTG
260 270 280 290 300
DSVTVAPAMT LTDWEYQRMR DLGIAILREV GVDTGGCNIQ FAINPHDGRL
310 320 330 340 350
IVIEMNPRVS RSSALASKAT GFPIAKIAVK LAVGYTLDEI LNDITKETPA
360 370 380 390 400
CFEPALDYVV VKAPRFAFEK FPGADPTLTT TMKSVGEAMS LGRNFVEALG
410 420 430 440 450
KVMRSLETGR FGFWTAPDPQ GDVDQVLLRL KTPTEGRLYD VELALRLGAS
460 470 480 490 500
TEKVAQVSGI DPWFVAQIGE LVKLRDELVA APVLDAELLR RAKHNGLSDR
510 520 530 540 550
QITALRPELL GEDGVRSLRK RLGIHPVYKT VDTCAAEFEA KTPYHYSSYE
560 570 580 590 600
LDPAAETEVV PQTEKPKVLI LGSGPNRIGQ GIEFDYSCVH AAITLSHNGF
610 620 630 640 650
ETVMVNCNPE TVSTDYDTAD RLYFEPLTFE DVLEVFYAEE QSAAGGAGVA
660 670 680 690 700
GVIVQLGGQT PLGLAQRLAD AGVPIVGTSP EAIDLAEDRG AFGDVLTAAG
710 720 730 740 750
LPAPKYGTAT TFAQARRIAA EIGYPVLVRP SYVLGGRGME IVYDEETLKD
760 770 780 790 800
YITRATALSH EHPVLVDRFL EDAVEIDVDA LCDGTEVYIG GVMEHIEEAG
810 820 830 840 850
IHSGDSACAL PPVTLGRSDL EKVRQATEAI ARGIGVVGLL NVQYALKEDV
860 870 880 890 900
LYVLEANPRA SRTVPFVSKA TAIPLAKACA RIMLGSSISQ LRFEGMLAAS
910 920 930 940 950
GDGGNVASHA PIAVKEAVLP FNRLRRADGA AIDSLLGPEM KSTGEVMGID
960 970 980 990 1000
HDFGRAFAKS QTAAYGSLPT QGTVFVSVAN RDKRLLVFPV KRLADLGFHV
1010 1020 1030 1040 1050
IATEGTAEML RRKGIPCDEV RKHFEPPKAG RPALSAVDAI RAGDVDMVIN
1060 1070 1080 1090 1100
TPYGNSGPRI DGYEIRSAAV SVNIPCVTTV QGASAAVQGI EAGIRGDIGV
1110 1120
RSLQELHSAI GAGIAADNEV Q
Length:1,121
Mass (Da):120,017
Last modified:August 2, 2002 - v2
Checksum:i2EABCB0A8D4281CD
GO

Sequence cautioni

The sequence CAC30044 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583918 Genomic DNA. Translation: CAC30044.1. Different initiation.
PIRiH86975.
RefSeqiNP_301455.2. NC_002677.1.
WP_010907779.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC30044; CAC30044; CAC30044.
GeneIDi909300.
KEGGimle:ML0536.
PATRICi18051980. VBIMycLep78757_0937.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583918 Genomic DNA. Translation: CAC30044.1. Different initiation.
PIRiH86975.
RefSeqiNP_301455.2. NC_002677.1.
WP_010907779.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ9CCR2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML0536.

Proteomic databases

PRIDEiQ9CCR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC30044; CAC30044; CAC30044.
GeneIDi909300.
KEGGimle:ML0536.
PATRICi18051980. VBIMycLep78757_0937.

Organism-specific databases

LepromaiML0536.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

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

Entry informationi

Entry nameiCARB_MYCLE
AccessioniPrimary (citable) accession number: Q9CCR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: September 7, 2016
This is version 99 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, 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.