P57244 (CARB_BUCAI) Reviewed, UniProtKB/Swiss-Prot

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:	BU144

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	1079 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.

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 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 1079	1078	Carbamoyl-phosphate synthase large chain HAMAP MF_01210_B		PRO_0000144995
Regions
	Domain	133 – 328	196	ATP-grasp 1
	Domain	679 – 870	192	ATP-grasp 2
	Nucleotide binding	159 – 216	58	ATP By similarity
	Nucleotide binding	705 – 762	58	ATP By similarity
	Region	2 – 403	402	Carboxyphosphate synthetic domain HAMAP MF_01210_B
	Region	404 – 553	150	Oligomerization domain HAMAP MF_01210_B
	Region	554 – 936	383	Carbamoyl phosphate synthetic domain HAMAP MF_01210_B
	Region	937 – 1079	143	Allosteric domain HAMAP MF_01210_B
Sites
	Metal binding	285	1	Magnesium or manganese 1 By similarity
	Metal binding	299	1	Magnesium or manganese 1 By similarity
	Metal binding	299	1	Magnesium or manganese 2 By similarity
	Metal binding	301	1	Magnesium or manganese 2 By similarity
	Metal binding	829	1	Magnesium or manganese 3 By similarity
	Metal binding	841	1	Magnesium or manganese 3 By similarity
	Metal binding	841	1	Magnesium or manganese 4 By similarity
	Metal binding	843	1	Magnesium or manganese 4 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57244 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 088D77AA95FD4217	FASTA	1,079	120,516
	10 20 30 40 50 60 MPKSTDIKSI LILGAGPIVI GQACEFDYSG TQACKALKEE GYRIILLNSN PATIMTDPDM 70 80 90 100 110 120 ADATYVEPIH WEIVEKIIQK EKPDALLPTM GGQTALNCAL ELDHKGILKK YGVQIIGATV 130 140 150 160 170 180 DAIKKAENRK LFEHSMKKLN LETAKCGIAH NIQEAFLVLN NVGFPCIIRP SFTMGGHGGG 190 200 210 220 230 240 IAYNHEEFEK ICERGLELSP STELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENLDPM 250 260 270 280 290 300 GIHTGDSITV APAQTLTDKE YQVMRNASMS ILREIGVETG GSNVQFAINP KNGRMIVIEM 310 320 330 340 350 360 NPRVSRSSAL ASKATGFPIA KIAAKLAIGY TLDELANDIT GTNTTASFEP SIDYIVTKIP 370 380 390 400 410 420 RFNFEKFPGC DDRLTTQMKS VGEVMAIGRT FQESIQKAIR GLEVGASGFD SKISSRDSEY 430 440 450 460 470 480 LIKIRRELKD AGSERIWYIG DAFRYGMSIN DVFDLTSIDP WFLVQIKEII LLEKKIIKNG 490 500 510 520 530 540 FIGLKYDFFY FLKRKGFSDQ RIAILTNKNE SEIRQLRYKL NLHPVYKRID TCSAEFSTET 550 560 570 580 590 600 AYMYSTWEDE CESHPSKNNK KIIILGGGPN RIGQGIEFDY CCVHAAQALR EDGFEAIMVN 610 620 630 640 650 660 CNPETVSTDY DISDRLYFEP ITLENVLEIV RIEKPKGVII QYGGQTPLKL AHEFEKEGVP 670 680 690 700 710 720 IIGTSPDSID TAENRYRFQK TVNKLRLQQP LNATVLTLDE AYKKADIIGY PIMVRPSYVL 730 740 750 760 770 780 GGRAMEIVYE PYGLENYFKT TLKKNNTTPI LLDQYLDYAT EVDVDAICDG ETVLIGGIME 790 800 810 820 830 840 HIEQAGVHSG DSACSLPAYT LTSKVQNEIR RQVKKLAFEL SVKGLMNIQF AIKNNKIYII 850 860 870 880 890 900 EVNPRAARTV PFVSKAIGLA LAKISVRVMC GKTLLEQGFI KEIIPPYFSV KEAVLPFDKF 910 920 930 940 950 960 QGVDPILGPE MRSTGEVMGI GKNFSEAFSK SMLGAHTNMK KSGRVLLSVR NNDKNNIINL 970 980 990 1000 1010 1020 AVKLKKLGFK IDATKGTSVA LKKSGISSRL VNKVHEGRPH IQDRLKNGEY SYIVNTTSCY 1030 1040 1050 1060 1070 QGIKDSKLIC RSALQYKVHY DTTVNGAFAT VMALNENPIK NIETLQKIHK KIQLFYTKK

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12862.1.
RefSeq	NP_239976.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57244.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000003156; EBBUCP00000002932; EBBUCG00000003156.
GeneID	1109588.
GenomeReviews	Gene locus BU144 in contig BA000003_GR.
KEGG	buc:BU144.
PATRIC	21243802. VBIBucAph127364_0153.
Phylogenomic databases
GeneTree	EBGT00050000008143.
HOGENOM	HBG405439.
OMA	QGVTKEI.
PhylomeDB	P57244.
ProtClustDB	PRK05294.
Enzyme and pathway databases
BioCyc	BSP107806:BU144-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. 2 hits. PS00867. CPSASE_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARB_BUCAI

Accession

Primary (citable) accession number: P57244

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program