Carbamoyl-phosphate synthase large chain

Preferred order of sections

Names and origin

Protein names

Recommended name:
Carbamoyl-phosphate synthase large chain
EC=6.3.5.5

Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain

Gene names

Name:	carB
Ordered Locus Names:	ML0536

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	1121 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	2 ATP + L-glutamine + HCO₃^- + H₂O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. HAMAP MF_01210_B
Cofactor	Binds 4 magnesium or manganese ions per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP MF_01210_B Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP MF_01210_B
Subunit structure	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 By similarity.
Sequence similarities	Belongs to the CarB family. Contains 2 ATP-grasp domains.
Sequence caution	The sequence CAC30044.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Pyrimidine biosynthesis
Domain	Repeat
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1121

1121

Carbamoyl-phosphate synthase large chain HAMAP MF_01210_B

PRO_0000145022

Regions

Domain

138 – 333

196

ATP-grasp 1

Domain

693 – 884

192

ATP-grasp 2

Nucleotide binding

164 – 221

58

ATP By similarity

Nucleotide binding

719 – 776

58

ATP By similarity

Region

1 – 407

407

Carboxyphosphate synthetic domain HAMAP MF_01210_B

Region

408 – 559

152

Oligomerization domain HAMAP MF_01210_B

Region

560 – 965

406

Carbamoyl phosphate synthetic domain HAMAP MF_01210_B

Region

966 – 1121

156

Allosteric domain HAMAP MF_01210_B

Sites

Metal binding

290

1

Magnesium or manganese 1 By similarity

Metal binding

304

1

Magnesium or manganese 1 By similarity

Metal binding

304

1

Magnesium or manganese 2 By similarity

Metal binding

306

1

Magnesium or manganese 2 By similarity

Metal binding

843

1

Magnesium or manganese 3 By similarity

Metal binding

855

1

Magnesium or manganese 3 By similarity

Metal binding

855

1

Magnesium or manganese 4 By similarity

Metal binding

857

1

Magnesium or manganese 4 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9CCR2 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: 2EABCB0A8D4281CD
Show »

FASTA

1,121

120,017

        10         20         30         40         50         60 
MPRRTDLNHV LVIGSGPIVI GQACEFDYAG TQACRVLRAE GLQVSLVNSN PATIMTDPEF 

        70         80         90        100        110        120 
ADHTYVEPIT PAFVERVIVQ QAERGNRIDA LLATLGGQTA LNTAVALYEN GVLERYGVEL 

       130        140        150        160        170        180 
IGADFEAIQR GEDRQRFKDL VAKVGGESAR SKVCFTMDEV RETVEDLGLP VVVRPSFTMG 

       190        200        210        220        230        240 
GLGSGMAHSD EEVGRMAGAG LVASPSANVL IEESVYGWKE FELELMRDGH DSVVVVCSIE 

       250        260        270        280        290        300 
NVDPMGVHTG DSVTVAPAMT LTDWEYQRMR DLGIAILREV GVDTGGCNIQ FAINPHDGRL 

       310        320        330        340        350        360 
IVIEMNPRVS RSSALASKAT GFPIAKIAVK LAVGYTLDEI LNDITKETPA CFEPALDYVV 

       370        380        390        400        410        420 
VKAPRFAFEK FPGADPTLTT TMKSVGEAMS LGRNFVEALG KVMRSLETGR FGFWTAPDPQ 

       430        440        450        460        470        480 
GDVDQVLLRL KTPTEGRLYD VELALRLGAS TEKVAQVSGI DPWFVAQIGE LVKLRDELVA 

       490        500        510        520        530        540 
APVLDAELLR RAKHNGLSDR QITALRPELL GEDGVRSLRK RLGIHPVYKT VDTCAAEFEA 

       550        560        570        580        590        600 
KTPYHYSSYE LDPAAETEVV PQTEKPKVLI LGSGPNRIGQ GIEFDYSCVH AAITLSHNGF 

       610        620        630        640        650        660 
ETVMVNCNPE TVSTDYDTAD RLYFEPLTFE DVLEVFYAEE QSAAGGAGVA GVIVQLGGQT 

       670        680        690        700        710        720 
PLGLAQRLAD AGVPIVGTSP EAIDLAEDRG AFGDVLTAAG LPAPKYGTAT TFAQARRIAA 

       730        740        750        760        770        780 
EIGYPVLVRP SYVLGGRGME IVYDEETLKD YITRATALSH EHPVLVDRFL EDAVEIDVDA 

       790        800        810        820        830        840 
LCDGTEVYIG GVMEHIEEAG IHSGDSACAL PPVTLGRSDL EKVRQATEAI ARGIGVVGLL 

       850        860        870        880        890        900 
NVQYALKEDV LYVLEANPRA SRTVPFVSKA TAIPLAKACA RIMLGSSISQ LRFEGMLAAS 

       910        920        930        940        950        960 
GDGGNVASHA PIAVKEAVLP FNRLRRADGA AIDSLLGPEM KSTGEVMGID HDFGRAFAKS 

       970        980        990       1000       1010       1020 
QTAAYGSLPT QGTVFVSVAN RDKRLLVFPV KRLADLGFHV IATEGTAEML RRKGIPCDEV 

      1030       1040       1050       1060       1070       1080 
RKHFEPPKAG RPALSAVDAI RAGDVDMVIN TPYGNSGPRI DGYEIRSAAV SVNIPCVTTV 

      1090       1100       1110       1120 
QGASAAVQGI EAGIRGDIGV RSLQELHSAI GAGIAADNEV Q

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References

[1]

"Massive gene decay in the leprosy bacillus."
Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S.

Barrell B.G.
Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TN.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL583918 Genomic DNA. Translation: CAC30044.1. Different initiation.
PIR	H86975.
RefSeq	NP_301455.2. NC_002677.1.
3D structure databases
ProteinModelPortal	Q9CCR2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000029076; EBMYCP00000028682; EBMYCG00000029071.
GeneID	909300.
GenomeReviews	Gene locus ML0536 in contig AL450380_GR.
KEGG	mle:ML0536.
NMPDR	fig\|272631.1.peg.327.
PATRIC	18051980. VBIMycLep78757_0937.
Organism-specific databases
Leproma	ML0536.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000015720.
HOGENOM	HBG405439.
ProtClustDB	PRK05294.
Enzyme and pathway databases
BioCyc	MLEP272631:ML0536-MONOMER.
Family and domain databases
HAMAP	MF_01210_B. CPSase_L_chain_B. [Tree]
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR006275. CarbamoylP_synth_lsu. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005483. CarbamoylP_synth_lsu_CPS-dom. IPR005481. CarbamoylP_synth_lsu_N. IPR005480. CarbamoylP_synth_lsu_oligo. IPR011607. MGS-like_dom. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 2 hits. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:1.10.1030.10. CarbamoylP_synth_lsu_oligo. 1 hit. G3DSA:3.40.50.1380. MGS-like_dom. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 2 hits.
KO	K01955.
Pfam	PF00289. CPSase_L_chain. 2 hits. PF02786. CPSase_L_D2. 2 hits. PF02787. CPSase_L_D3. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PRINTS	PR00098. CPSASE.
SMART	SM01096. CPSase_L_D3. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF48108. CarbamoylP_synth_lsu_oligo. 1 hit. SSF52335. MGS-like_dom. 1 hit. SSF52440. PreATP-grasp-like. 2 hits.
TIGRFAMs	TIGR01369. CPSaseII_lrg. 1 hit.
PROSITE	PS50975. ATP_GRASP. 2 hits. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARB_MYCLE

Accession

Primary (citable) accession number: Q9CCR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	August 2, 2002
Last modified:	January 25, 2012
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents