Carbamoyl-phosphate synthase large chain - Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)

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:	SAG1042

Organism

Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R) [Complete proteome] [HAMAP]

Taxonomic identifier

208435 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length	1060 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-Rule MF_01210
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-Rule MF_01210 Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP-Rule MF_01210
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.

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	'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1060

1060

Carbamoyl-phosphate synthase large chain HAMAP-Rule MF_01210

PRO_0000145048

Regions

Domain

133 – 327

195

ATP-grasp 1

Domain

671 – 861

191

ATP-grasp 2

Nucleotide binding

159 – 216

58

ATP By similarity

Nucleotide binding

697 – 754

58

ATP By similarity

Region

1 – 401

401

Carboxyphosphate synthetic domain HAMAP-Rule MF_01210

Region

402 – 546

145

Oligomerization domain HAMAP-Rule MF_01210

Region

547 – 929

383

Carbamoyl phosphate synthetic domain HAMAP-Rule MF_01210

Region

930 – 1060

131

Allosteric domain HAMAP-Rule MF_01210

Sites

Metal binding

284

1

Magnesium or manganese 1 By similarity

Metal binding

298

1

Magnesium or manganese 1 By similarity

Metal binding

298

1

Magnesium or manganese 2 By similarity

Metal binding

300

1

Magnesium or manganese 2 By similarity

Metal binding

820

1

Magnesium or manganese 3 By similarity

Metal binding

832

1

Magnesium or manganese 3 By similarity

Metal binding

832

1

Magnesium or manganese 4 By similarity

Metal binding

834

1

Magnesium or manganese 4 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8DZQ7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 04C6D2B617E08274
Show »

FASTA

1,060

117,093

        10         20         30         40         50         60 
MPKRTDIRKI MVIGSGPIVI GQAAEFDYSG TQACLSLKEE GYQVVLVNSN PATIMTDKDI 

        70         80         90        100        110        120 
ADKVYIEPIT LEFVTRILRK ERPDALLPTL GGQTGLNMAM ALSKNGILEE LNVELLGTKL 

       130        140        150        160        170        180 
SAIDKAEDRD LFKQLMEELN QPIPESEIVN SVEEAIQFAE QIGYPLIVRP AFTLGGTGGG 

       190        200        210        220        230        240 
MCDNQEQLVD ITTKGLKLSP VTQCLIERSI AGFKEIEYEV MRDAADNALV VCNMENFDPV 

       250        260        270        280        290        300 
GIHTGDSIVF APAQTLSDVE NQLLRDASLD IIRALKIEGG CNVQLALDPN SFKYYVIEVN 

       310        320        330        340        350        360 
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVINPITK TTYAMFEPAL DYVVAKMPRF 

       370        380        390        400        410        420 
PFDKFESGDR KLGTQMKATG EVMAIGRNIE ESLLKACRSL EIGVDHIKIA DLDNVSDDVL 

       430        440        450        460        470        480 
LEKIRKAEDD RLFYLAEALR RHYSIEKLAS LTSIDSFFLD KLRVIVELED LLSKNRLDIN 

       490        500        510        520        530        540 
ILKKVKNKGF SDKAIASLWQ INEDQVRNMR KEAGILPVYK MVDTCASEFD SATPYFYSTY 

       550        560        570        580        590        600 
AVENESLISD KASILVLGSG PIRIGQGVEF DYATVHSVKA IRESGFEAII MNSNPETVST 

       610        620        630        640        650        660 
DFSISDKLYF EPLTFEDVMN VIDLEKPEGV ILQFGGQTAI NLAKDLNKAG VKILGTQLED 

       670        680        690        700        710        720 
LDRAENRKQF EATLQALNIP QPPGFTATTE EEAVNAAQKI GYPVLVRPSY VLGGRAMKIV 

       730        740        750        760        770        780 
ENEEDLRHYM TTAVKASPDH PVLIDAYLIG KECEVDAISD GQNILIPGIM EHIERSGVHS 

       790        800        810        820        830        840 
GDSMAVYPPQ TLSETIIETI VDYTKRLAIG LNCIGMMNIQ FVIKDQKVYV IEVNPRASRT 

       850        860        870        880        890        900 
LPFLSKVTHI PMAQVATKVI LGDKLCNFTY GYDLYPASDM VHIKAPVFSF TKLAKVDSLL 

       910        920        930        940        950        960 
GPEMKSTGEV MGSDINLQKA LYKAFEAAYL HMPDYGNIVF TVDDTDKEEA LELAKVYQSI 

       970        980        990       1000       1010       1020 
GYRIYATQGT AIYFDANGLE TVLVGKLGEN DRNHIPDLIK NGKIQAVINT VGQNNIDNHD 

      1030       1040       1050       1060 
ALIIRRSAIE QGVPLFTSLD TAHAMFKVLE SRAFTLKVLD

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References

[1]

"Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae."
Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N., Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F.

Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-611 / 2603 V/R.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009948 Genomic DNA. Translation: AAM99924.1.
RefSeq	NP_688052.1. NC_004116.1.
3D structure databases
ProteinModelPortal	Q8DZQ7.
ModBase	Search...
Protein-protein interaction databases
STRING	208435.SAG1042.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM99924; AAM99924; SAG1042.
GeneID	1013846.
KEGG	sag:SAG1042.
PATRIC	19628924. VBIStrAga72745_1053.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0458.
HOGENOM	HOG000234582.
KO	K01955.
OMA	PMANLAT.
ProtClustDB	PRK05294.
Enzyme and pathway databases
BioCyc	SAGA208435:GHVY-1043-MONOMER.
UniPathway	UPA00068; UER00171. UPA00070; UER00115.
Family and domain databases
Gene3D	1.10.1030.10. 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.
HAMAP	MF_01210_B. CPSase_L_chain_B.
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR006275. CarbamoylP_synth_lsu. IPR005481. CarbamoylP_synth_lsu_N. 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]
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. 2 hits. PS00867. CPSASE_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARB_STRA5

Accession

Primary (citable) accession number: Q8DZQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 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

Protein-protein interaction 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