Q75D66 (CARB_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Arginine-specific carbamoyl-phosphate synthetase, ammonia chain

Gene names

Name:	CPA2
Ordered Locus Names:	ABR157W

Organism

Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

284811 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

Protein attributes

Sequence length	1113 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.
Cofactor	Binds 3 manganese ions per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
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.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	In eukaryotes this enzyme is synthesized by two pathway-specific (arginine and pyrimidine) under separate control.
Sequence similarities	Belongs to the CarB family. Contains 2 ATP-grasp domains.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding 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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 1113	1113	Carbamoyl-phosphate synthase arginine-specific large chain		PRO_0000145088
Regions
	Domain	154 – 346	193	ATP-grasp 1
	Domain	693 – 888	196	ATP-grasp 2
	Nucleotide binding	174 – 229	56	ATP Potential
	Nucleotide binding	321 – 371	51	ATP Potential
Sites
	Metal binding	303	1	Manganese 1 By similarity
	Metal binding	317	1	Manganese 1 By similarity
	Metal binding	317	1	Manganese 2 By similarity
	Metal binding	319	1	Manganese 2 By similarity
	Metal binding	843	1	Manganese 3 By similarity
	Metal binding	859	1	Manganese 3 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q75D66 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: FE979E5C405A507D	FASTA	1,113	121,650
	10 20 30 40 50 60 MSTAGISDEA SASAFTTAGY CPQLIKGIDS VLIIGSGGLS IGQAGEFDYS GSQAIKALKE 70 80 90 100 110 120 TGKRTILINP NIATNQTSYS LADEVYFLPV TPEFITHVIK RERPDGILLT FGGQTGLNCG 130 140 150 160 170 180 VALQRAVTLE KYGVTVLGTP ISVLETTEDR ELFARALKEI NMPIAESVAC STVEDAVAAA 190 200 210 220 230 240 NDIGYPVIVR SAYALGGLGS GFADDDLQLR QLCAQSLALS PQVLVEKSLK GWKEIEYEVV 250 260 270 280 290 300 RDRVGNCITV CNMENFDPLG IHTGDSIVLA PSQTLSDEEF HMLRTAAIEI IRHLGVVGEC 310 320 330 340 350 360 NVQYALQPDG LAFKVIEVNA RLSRSSALAS KATGYPLAYT AAKIALGYTL PELPNPVTKS 370 380 390 400 410 420 TVANFEPSLD YIVAKVPRWD LSKFQHVDKT IGSAMKSVGE VMAIGRNFEE AFQKAFRQVD 430 440 450 460 470 480 PSLLGFQGSD EFADLDEALQ FPTDRRWLAV GEALMNRGYS VERVHELTKI DRFFLHKCMN 490 500 510 520 530 540 IVRMQKQLET LGSINRLDEV LLRKAKKLGF CDKQIARAIS DDLSELDIRA LRKSFGILPF 550 560 570 580 590 600 VKRIDTMAAE VPAVTNYLYV TYNAVKDDVT FGDNGIMVLG SGVYRIGSSV EFDWCAVNTV 610 620 630 640 650 660 QALRKEGHKT IMINYNPETV STDFDEVDRL YFEELSFERV MDIYEAECAS GCVISMGGQQ 670 680 690 700 710 720 PQNIASQLYE QGANILGTSP EDIDKAEDRH KFSTILDTLG LDQPRWSELK SLSEVKHFLD 730 740 750 760 770 780 DVGYPVLVRP SYVLSGAAMS TVYNSEDLEG VFESAVAVSP EHPVVISKFI EGAQELDIDA 790 800 810 820 830 840 VAYKGSLLVH AISEHVENAG VHSGDATLVL PPQSLKEEEK TRLKQLAAQV AAAWNITGPF 850 860 870 880 890 900 NMQIIKTAEG GHTCLKIIEC NIRASRSFPF VSKVLGVNFV EIAVKAFLGG DLVPPSCDLM 910 920 930 940 950 960 ARSYNYVATK CPQFSFTRLP GADPFLGVEM ASVGEVAAFG SNALESYWVA LQGLMSFCVP 970 980 990 1000 1010 1020 LPPSGILLGG DLSKEHLGRV AALLAPHGFT LLALSEATCE YLSRYLPAES SVTVLQMPET 1030 1040 1050 1060 1070 1080 GREVRALFEQ HNVQCVVNLA ARRASSPIDP DYRIRRSAID FAVPLFNEPQ TTMLFARALS 1090 1100 1110 AYLPAELEMR QSDGPETPSY VLPWREYLGF KPT

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016815 Genomic DNA. Translation: AAS50929.1.
RefSeq	NP_983105.2. NM_208458.2.
3D structure databases
ProteinModelPortal	Q75D66.
ModBase	Search...
Protein-protein interaction databases
STRING	Q75D66.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4619215.
GenomeReviews	Gene locus ABR157W in contig AE016815_GR.
KEGG	ago:AGOS_ABR157W.
NMPDR	fig|33169.1.peg.750.
Organism-specific databases
AGD	ABR157W.
Phylogenomic databases
eggNOG	fuNOG06096.
HOGENOM	HBG405439.
OMA	EGIEVAN.
OrthoDB	EOG4T7CBC.
PhylomeDB	Q75D66.
Family and domain databases
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. [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_ASHGO

Accession

Primary (citable) accession number: Q75D66

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program