Reviewed, UniProtKB/Swiss-Prot Q58976 (PYRB_METJA)

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:	MJ1581

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	306 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	Heterododecamer (2C3:3R2) of six catalytic pyrB chains organized as two trimers (C3), and six regulatory pyrI chains organized as three dimers (R2). 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 306	306	Aspartate carbamoyltransferase HAMAP MF_00001		PRO_0000113247

Sequences

	Sequence		Length	Mass (Da)
	Q58976-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CBDC31FC450CEF6A	FASTA	306	35,160
	10 20 30 40 50 60 MKHLISMKDI GKEEILEILD EARKMEELLN TKRPLKLLEG KILATVFYEP STRTRLSFET 70 80 90 100 110 120 AMKRLGGEVI TMTDLKSSSV AKGESLIDTI RVISGYADII VLRHPSEGAA RLASEYSQVP 130 140 150 160 170 180 IINAGDGSNQ HPTQTLLDLY TIMREIGRID GIKIAFVGDL KYGRTVHSLV YALSLFENVE 190 200 210 220 230 240 MYFVSPKELR LPKDIIEDLK AKNIKFYEKE SLDDLDDDID VLYVTRIQKE RFPDPNEYEK 250 260 270 280 290 300 VKGSYKIKRE YVEGKKFIIM HPLPRVDEID YDVDDLPQAK YFKQSFYGIP VRMAILKKLI EDNEGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Characterization of the aspartate transcarbamoylase from Methanococcus jannaschii." Hack E.S., Vorobyova T., Sakash J.B., West J.M., Macol C.P., Herve G., Williams M.K., Kantrowitz E.R. J. Biol. Chem. 275:15820-15827(2000) [PubMed: 10748118] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Crystallization and structure determination of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase." Vitali J., Vorobyova T., Webster G., Kantrowitz E.R. Acta Crystallogr. D 56:1061-1063(2000) [PubMed: 10944354] [Abstract] Cited for: CRYSTALLIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L77117 Genomic DNA. Translation: AAB99601.1.

PIR

D64497.

RefSeq

NP_248590.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RGW	X-ray	2.80	A/B/C/D/E/F	1-306	[»]
3E2P	X-ray	3.00	A/B/C/D/E/F/I/J/K/L/M/N	1-306	[»]

ModBase

Search...

Genome annotation databases

GeneID

1452490.

GenomeReviews

Gene locus MJ1581 in contig L77117_GR.

KEGG

mja:MJ1581.

NMPDR

fig|243232.1.peg.1627.

TIGR

MJ1581.

Phylogenomic databases

HOGENOM

Q58976.

OMA

Q58976. RFDESEY.

Enzyme and pathway databases

BioCyc

MJAN243232:MJ_1581-MON.

BRENDA

2.1.3.2. 256362.

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_METJA

Accession

Primary (citable) accession number: Q58976

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
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)