Q9HK17 (CARB_THEAC) 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:	Ta0791

Organism

Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

Taxonomic identifier

273075 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma

Protein attributes

Sequence length	1047 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_A
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_A Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP MF_01210_A
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
	Chain	1 – 1047	1047	Carbamoyl-phosphate synthase large chain HAMAP MF_01210_A		PRO_0000145086
Regions
	Domain	133 – 325	193	ATP-grasp 1
	Domain	665 – 854	190	ATP-grasp 2
	Nucleotide binding	159 – 216	58	ATP By similarity
	Nucleotide binding	691 – 746	56	ATP By similarity
	Region	1 – 398	398	Carboxyphosphate synthetic domain HAMAP MF_01210_A
	Region	399 – 539	141	Oligomerization domain HAMAP MF_01210_A
	Region	540 – 916	377	Carbamoyl phosphate synthetic domain HAMAP MF_01210_A
	Region	916 – 1047	132	Allosteric domain HAMAP MF_01210_A
Sites
	Metal binding	284	1	Magnesium or manganese 1 By similarity
	Metal binding	296	1	Magnesium or manganese 1 By similarity
	Metal binding	296	1	Magnesium or manganese 2 By similarity
	Metal binding	298	1	Magnesium or manganese 2 By similarity
	Metal binding	813	1	Magnesium or manganese 3 By similarity
	Metal binding	825	1	Magnesium or manganese 3 By similarity
	Metal binding	825	1	Magnesium or manganese 4 By similarity
	Metal binding	827	1	Magnesium or manganese 4 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HK17 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: E062CAD131746864	FASTA	1,047	116,852
	10 20 30 40 50 60 MPRRDDIHRI LVIGSGPVVI GQAAEFDYSG SQACLSLREE GYYVVLLNSN PATIQTDHRI 70 80 90 100 110 120 ADRVYIEPIT VEAVERIIEK EKIDAIEPHM GGQTALNLAV KLKNSGILQR YGIKIIGTPV 130 140 150 160 170 180 ESIELAEDRE KFYEFLKAMG EPQPARYRIR RDHIDEDVAS IPDIPVIVRT SFSLGGTGGS 190 200 210 220 230 240 IVQNRQDLLA MAENLFRASD IDYLEVNESL EGMKEIEYEV IRDSFGNCIT VCNMENLDPM 250 260 270 280 290 300 GVHTGESIVV TPSQTLSDIE YQMLRDSAIR IISGLGIEGA CNIQFALSEG RYYVIEVNPR 310 320 330 340 350 360 TSRSSALASK ATGYPIARIA AKIAAGYGLH EIKNPITKST FAAYEPSLDY VTVKIPRWPF 370 380 390 400 410 420 DKFSVDRTIG VQMKSIGEVM GIGRTFEEAL MKAIASLDNA FSSNIRLHVP DDELWRLIGK 430 440 450 460 470 480 PNDRRIFAIF EGLFRNFDVK RMSRLSGYDE YFIEKMRNIV EALRNMDMGR IPENLLRIKR 490 500 510 520 530 540 IGIPDEIISA FCGVPADTIT KYRIDRNIMP VYKRIDTCSG EFEVAVPYMY STYEDEDETP 550 560 570 580 590 600 DLSGSIMIIG SGPNRIAQGL EFDYGSVKAI LALRDMGYRS IMLNSNPETV STDFDISDAL 610 620 630 640 650 660 FFEPVTPEYV VNVIRRSGCA GLIVQFSGQT GQNMARRIEE ILGKHIVLGT STESIDRIED 670 680 690 700 710 720 RTVFSRVIEG LGIKQPPFAI AENENDTVRK AMGLGLPIIL RSSHVIGGRS MEIIYDVDYL 730 740 750 760 770 780 ADRAREIFAI SKNVLVSKYL ENAVEMDVDF VSDGTSYSIC GIIVHIEEAG VHSGDATMVY 790 800 810 820 830 840 GPGIVPVDIE KKIEGIVGSM VREFRLIGLS NLQIAVRDGD VYVIELNARS SRSVPFISKA 850 860 870 880 890 900 TGIDWVRLAV ECMIGSRIEN KRMEAKSYFL KVSVFPFSKF SDMDVVYGPE MKSTGEAMYP 910 920 930 940 950 960 GRTLAEALRK SLQRSISSVL ITVRDEDKPR IVDIARILLE KGVKLYATAG TSKFLADHGI 970 980 990 1000 1010 1020 PTETLYRVRD RREPRILDMI SSGSIDMVIN TTEMTAGAVR DGFKIRRICI MRGIPLIMNI 1030 1040 NLARAYAEAL GQVEVDYREI GDYLQVS

References

[1]	"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum." Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W. Nature 407:508-513(2000) [PubMed: 11029001] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL445065 Genomic DNA. Translation: CAC11922.1.
RefSeq	NP_394253.1. NC_002578.1.
3D structure databases
ProteinModelPortal	Q9HK17.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1456343.
GenomeReviews	Gene locus Ta0791 in contig AL139299_GR.
KEGG	tac:Ta0791.
NMPDR	fig|273075.1.peg.775.
Phylogenomic databases
HOGENOM	HBG405439.
OMA	VIIRPAF.
ProtClustDB	PRK05294.
Enzyme and pathway databases
BioCyc	TACI273075:TA0791-MONOMER.
Family and domain databases
HAMAP	MF_01210_A. CPSase_L_chain_A. [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. False negative. PS00867. CPSASE_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CARB_THEAC

Accession

Primary (citable) accession number: Q9HK17

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
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