Reviewed, UniProtKB/Swiss-Prot Q55338 (PYRB_SULAC)

Names and origin

Protein names

Recommended name:
    Aspartate carbamoyltransferase
    EC=2.1.3.2
Alternative name(s):
    Aspartate transcarbamylase
      Short name=ATCase

Gene names

Name:	pyrB
Ordered Locus Names:	Saci_1596

Organism

Sulfolobus acidocaldarius [Complete proteome] [HAMAP]

Taxonomic identifier

2285 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. HAMAP MF_00001
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6. HAMAP MF_00001
Subunit structure	Heterooligomer of catalytic and regulatory chains. HAMAP MF_00001
Sequence similarities	Belongs to the ATCase/OTCase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro amino acid metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pyrI	P74766	1	EBI-1039019,EBI-1039029

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

Aspartate carbamoyltransferase HAMAP MF_00001

PRO_0000113258

Secondary structure

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299

Helix Strand Turn

Details...

Helix

7 – 9

3

Helix

12 – 26

15

Turn

35 – 38

4

Beta strand

40 – 47

8

Helix

50 – 62

13

Beta strand

66 – 71

6

Helix

84 – 94

11

Beta strand

96 – 105

10

Helix

107 – 114

8

Beta strand

119 – 124

6

Turn

125 – 127

3

Helix

130 – 144

15

Beta strand

151 – 156

6

Helix

162 – 170

9

Helix

171 – 173

3

Beta strand

177 – 182

6

Helix

185 – 187

3

Helix

191 – 194

4

Beta strand

201 – 205

5

Helix

207 – 209

3

Helix

211 – 213

3

Beta strand

215 – 220

6

Helix

230 – 236

7

Helix

237 – 240

4

Helix

244 – 248

5

Beta strand

255 – 257

3

Beta strand

263 – 266

4

Helix

268 – 272

5

Helix

278 – 297

20

Sequences

	Sequence		Length	Mass (Da)
	Q55338-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6A283A584F94E32D	FASTA	299	34,171
	10 20 30 40 50 60 MKHIISAYNF SRDELEDIFA LTDKYSKNLN DTRKILSGKT ISIAFFEPST RTYLSFQKAI 70 80 90 100 110 120 INLGGDVIGF SGEESTSVAK GENLADTIRM LNNYSDGIVM RHKYDGASRF ASEISDIPVI 130 140 150 160 170 180 NAGDGKHEHP TQAVIDIYTI NKHFNTIDGL VFALLGDLKY ARTVNSLLRI LTRFRPKLVY 190 200 210 220 230 240 LISPQLLRAR KEILDELNYP VKEVENPFEV INEVDVLYVT RIQKERFVDE MEYEKIKGSY 250 260 270 280 290 IVSLDLANKM KKDSIILHPL PRVNEIDRKV DKTTKAKYFE QASYGVPVRM SILTKIYGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification and characterization." Durbecq V., Thia-Toong T.-L., Charlier D.R.M., Villeret V., Roovers M., Wattiez R., Legrain C., Glansdorff N. Eur. J. Biochem. 264:233-241(1999) [PubMed: 10447693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770.
[2]	"Genes of de novo pyrimidine biosynthesis from the hyperthermoacidophilic crenarchaeote Sulfolobus acidocaldarius: novel organization in a bipolar operon." Thia-Toong T.-L., Roovers M., Durbecq V., Gigot D., Glansdorff N., Charlier D.R.M. J. Bacteriol. 184:4430-4441(2002) [PubMed: 12142413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770.
[3]	"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota." Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A. J. Bacteriol. 187:4992-4999(2005) [PubMed: 15995215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X99872 Genomic DNA. Translation: CAA68165.1.
AJ459777 Genomic DNA. Translation: CAD31976.1.
CP000077 Genomic DNA. Translation: AAY80909.1.

RefSeq

YP_256202.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PG5	X-ray	2.60	A	2-299	[»]
2BE9	X-ray	2.60	A	2-299	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q55338. 1 interaction.

Genome annotation databases

GeneID

3474279.

GenomeReviews

Gene locus Saci_1596 in contig CP000077_GR.

KEGG

sai:Saci_1596.

NMPDR

fig|330779.3.peg.513.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q55338.

OMA

Q55338. RFDESEY.

Enzyme and pathway databases

BioCyc

SACI330779:SACI_1596-MON.

BRENDA

2.1.3.2. 434.

Family and domain databases

HAMAP

MF_00001.
[Tree]

InterPro

IPR006132. Asp/Orn_carbamoyltranf_P_bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082. Aspartate_carbamoyltransf_euk.
[Graphical view]

Pfam

PF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]

PRINTS

PR00100. AOTCASE.
PR00101. ATCASE.

TIGRFAMs

TIGR00670. asp_carb_tr. 1 hit.

PROSITE

PS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PYRB_SULAC

Accession

Primary (citable) accession number: Q55338
Secondary accession number(s): Q4J8H1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)