Carbamoyl-phosphate synthase large chain - Rhizobium meliloti (strain 1021) (Ensifer meliloti)

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:	R01576
ORF Names:	SMc01215

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium ›

Protein attributes

Sequence length	1163 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 – 1163

1163

Carbamoyl-phosphate synthase large chain HAMAP-Rule MF_01210

PRO_0000145033

Regions

Domain

185 – 381

197

ATP-grasp 1

Domain

743 – 955

213

ATP-grasp 2

Nucleotide binding

212 – 269

58

ATP By similarity

Nucleotide binding

769 – 847

79

ATP By similarity

Region

1 – 456

456

Carboxyphosphate synthetic domain HAMAP-Rule MF_01210

Region

457 – 614

158

Oligomerization domain HAMAP-Rule MF_01210

Region

615 – 1026

412

Carbamoyl phosphate synthetic domain HAMAP-Rule MF_01210

Region

1027 – 1163

137

Allosteric domain HAMAP-Rule MF_01210

Sites

Metal binding

338

1

Magnesium or manganese 1 By similarity

Metal binding

352

1

Magnesium or manganese 1 By similarity

Metal binding

352

1

Magnesium or manganese 2 By similarity

Metal binding

354

1

Magnesium or manganese 2 By similarity

Metal binding

914

1

Magnesium or manganese 3 By similarity

Metal binding

926

1

Magnesium or manganese 3 By similarity

Metal binding

926

1

Magnesium or manganese 4 By similarity

Metal binding

928

1

Magnesium or manganese 4 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q92PZ4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 24B1EC4528C8124B
Show »

FASTA

1,163

126,002

        10         20         30         40         50         60 
MPKRQDIKSI LIIGAGPIVI GQACEFDYSG TQACKALKEE GYRVILVNSN PATIMTDPGL 

        70         80         90        100        110        120 
ADATYVEPIT PEVVAKIIAK ERPDALLPTM GGQTALNTAL SLRRMGVLDR YNVEMIGAKP 

       130        140        150        160        170        180 
EAIDKAEDRA LFREAMAHIG LETPKSRLAN ATDIKDHDRK SHEAERSALK AKLSGDELDK 

       190        200        210        220        230        240 
ALDELENQWN LGEGDRKQRY VNHAMAIAAQ ALDDVGLPAI IRPSFTLGGT GGGIAYNRSE 

       250        260        270        280        290        300 
FFEIVGSGLD ASPTTEVLIE ESVLGWKEYE MEVVRDKADN CIIICSIENI DPMGVHTGDS 

       310        320        330        340        350        360 
ITVAPALTLT DKEYQIMRNA SIAVLREIGV ETGGSNVQFA VNPENGRLVV IEMNPRVSRS 

       370        380        390        400        410        420 
SALASKATGF PIAKIAAKLA VGYTLDELEN DITGGATPAS FEPSIDYVVT KIPRFAFEKF 

       430        440        450        460        470        480 
PGAEPTLTTA MKSVGEVMAI GRTFAESLQK ALRGLETGLT GLDEIEVPDF DDNGDGRNAI 

       490        500        510        520        530        540 
RAALGTPTPD RLRMVAQALR LGMSEAEVHE ACKIDPWFIA QFKAIVDMEA RIREHGLPAD 

       550        560        570        580        590        600 
AENLRMLKAM GFSDARLATL TGKRPKEVAE LRNALNVRPV YKRIDTCAAE FASPTAYMYS 

       610        620        630        640        650        660 
TYETPFVGAA RSEAQVSDRK KVVILGGGPN RIGQGIEFDY CCCHAAFALK DAGYEAIMIN 

       670        680        690        700        710        720 
CNPETVSTDY DTSDRLYFEP LTAEDVIEIM RAEQENGTLH GVIVQFGGQT PLKLAEALEK 

       730        740        750        760        770        780 
NGIPILGTAP DAIDLAEDRD RFQKLLMKLD LNQPNNGIAY SVEQARLVAG EIGFPLVVRP 

       790        800        810        820        830        840 
SYVLGGRAMQ IIHSESMLQS YLLDTVPGLV PEDIKQRYPN DKTGQINTLL GKNPLLFDSY 

       850        860        870        880        890        900 
LTNAIEVDVD CLCDGKDVFV SGIMEHIEEA GIHSGDSACS LPVHSLGTDM VDELERQTGA 

       910        920        930        940        950        960 
LARALNVGGL MNVQFAIKDG TIYVLEVNPR ASRTVPFVAK TIGAPIAKIA ARVMAGEMLD 

       970        980        990       1000       1010       1020 
EAIAAYGKKP NPRNLKHIAV KEAVFPFARF PGVDTLLGPE MRSTGEVIGL DTDYALAFAK 

      1030       1040       1050       1060       1070       1080 
SQLGAGVDLP RDGTVFVSVR DEDKERVLPA IRILSDIGFK VMATGGTARF LGEQGIVATK 

      1090       1100       1110       1120       1130       1140 
INKVLEGRPH VEDAIRNRQV QLVINTTDGN KAISDSKSLR RATLMQKVPY YTTMAGAEAA 

      1150       1160 
ALAIKALKAG NLEVRPLQSY FET

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References

[1]

"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.

Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

[2]

"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A.

Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC46155.1.
RefSeq	NP_385682.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q92PZ4.
ModBase	Search...
Protein-protein interaction databases
STRING	266834.SMc01215.
Proteomic databases
PRIDE	Q92PZ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC46155; CAC46155; SMc01215.
GeneID	1233230.
KEGG	sme:SMc01215.
PATRIC	23632505. VBISinMel96828_3003.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0458.
HOGENOM	HOG000234582.
KO	K01955.
OMA	SEFFEIV.
ProtClustDB	PRK05294.
Enzyme and pathway databases
BioCyc	SMEL266834:GJF6-1612-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. 3 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_RHIME

Accession

Primary (citable) accession number: Q92PZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 88 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

Proteomic 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