O67233 (CARB2_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbamoyl-phosphate synthase large chain, C-terminal section
EC=6.3.5.5

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

Gene names

Name:	carB2
Ordered Locus Names:	aq_1172

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	537 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 2 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.
Domain	Corresponds to the C-terminal section. HAMAP MF_01210_B
Sequence similarities	Belongs to the CarB family. Contains 1 ATP-grasp domain.
Caution	CarB is split into two genes in A.aeolicus (AQ_1172 and AQ_2101).

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Pyrimidine biosynthesis
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference 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 – 537	537	Carbamoyl-phosphate synthase large chain, C-terminal section HAMAP MF_01210_B		PRO_0000144985
Regions
	Domain	122 – 313	192	ATP-grasp
	Nucleotide binding	148 – 205	58	ATP By similarity
	Region	1 – 397	397	Carbamoyl phosphate synthetic domain HAMAP MF_01210_B
	Region	398 – 537	140	Allosteric domain HAMAP MF_01210_B
Sites
	Metal binding	272	1	Magnesium or manganese 1 By similarity
	Metal binding	284	1	Magnesium or manganese 1 By similarity
	Metal binding	284	1	Magnesium or manganese 2 By similarity
	Metal binding	286	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O67233 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 9C777FD2ED8085F6	FASTA	537	60,037
	10 20 30 40 50 60 MSKKVVILGS GPNRIGQGIE FDYACVHAVF SLQEEGYYAV MVNCNPETVS TDYDTADKLY 70 80 90 100 110 120 FEPIVFEHVM DIIEREKPEG VILQFGGQTP LKLALPLQKN GVKILGTKPE SIDKAEDREL 130 140 150 160 170 180 FRELIIELGL KQPPSGTART KEEALKIAKE IGFPVLVRPS YVLGGRAMRI VYDEEELKEY 190 200 210 220 230 240 LEEAVSVSHE RPVLIDKFLD NSIELDVDAV SDGKDVLIGA VMEHIEEAGV HSGDSATSIP 250 260 270 280 290 300 PYSLSKEIVE EVKEQTRKLA VALEVKGLIN VQYAVQNNEV YVLEVNPRAS RTVPFVSKSI 310 320 330 340 350 360 GYPLAKIATK VAIGKSLREI LPEVFERLEK GEAHFASDFL PKEKKIFSVK EVVFPWKRFP 370 380 390 400 410 420 EVDPILGPEM KSTGEVMGID KEFGLAYYKA QLSAGYRLPE KGNLFISVAD RDKPKILELA 430 440 450 460 470 480 KEFEKLGFGI YATSGTYKFL KEHGVNAKRV LKVSEGRPNV VDMIINGEIH LVINTPSGKR 490 500 510 520 530 EKSDAYYIRR ACVQFNVPYY TTMRAGYAVL EAIKSIKKLK EEGKGLSVHS LQEIYNI

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC07203.1.
PIR	F70400.
RefSeq	NP_213797.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O67233.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1192579.
GenomeReviews	Gene locus aq_1172 in contig AE000657_GR.
KEGG	aae:aq_1172.
NMPDR	fig|224324.1.peg.812.
PATRIC	20959582. VBIAquAeo85532_0911.
Phylogenomic databases
HOGENOM	HBG405439.
OMA	CVQAVFA.
PhylomeDB	O67233.
ProtClustDB	CLSK382519.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_1172-MONOMER.
Family and domain databases
HAMAP	MF_01210_B. CPSase_L_chain_B. Divergent sequence. [Tree]
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005483. CarbamoylP_synth_lsu_CPS-dom. IPR005481. CarbamoylP_synth_lsu_N. IPR011607. MGS-like_dom. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.1380. MGS-like_dom. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KO	K01955.
Pfam	PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PRINTS	PR00098. CPSASE.
SMART	SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF52335. MGS-like_dom. 1 hit. SSF52440. PreATP-grasp-like. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARB2_AQUAE

Accession

Primary (citable) accession number: O67233

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
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