N5-carboxyaminoimidazole ribonucleotide mutase

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Q81ZH8 (Q81ZH8_BACAN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
N5-carboxyaminoimidazole ribonucleotide mutase PIRNR PIRNR001338
Short name=N5-CAIR mutase PIRNR PIRNR001338
EC=5.4.99.18 PIRNR PIRNR001338

Gene names

Name:	purE EMBL AAP24324.1
Ordered Locus Names:	BA_0288 EMBL AAP24324.1, BAS0275 EMBL AAT52606.1, GBAA_0288 EMBL AAT29375.1

Organism

Bacillus anthracis [Reference proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) By similarity. PIRNR PIRNR001338
Catalytic activity	5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. PIRNR PIRNR001338
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. PIRNR PIRNR001338
Sequence similarities	Belongs to the AIR carboxylase family. PIRNR PIRNR001338

Ontologies

Keywords
Biological process	Purine biosynthesis PIRNR PIRNR001338
Molecular function	Isomerase PIRNR PIRNR001338 Lyase EMBL AAP24324.1
Technical term	3D-structure PDB 1XMP PDB 4AY4 PDB 4B4K PDB 4AY3 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	5-(carboxyamino)imidazole ribonucleotide mutase activity Inferred from electronic annotation. Source: EC lyase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Binding site

Substrate By similarity PIRSR PIRSR001338-1

Binding site

Substrate By similarity PIRSR PIRSR001338-1

Binding site

Substrate By similarity PIRSR PIRSR001338-1

Sequences

Sequence

Length

Mass (Da)

Tools

Q81ZH8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6BC2A80C2A91A94E
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FASTA

161

17,042

        10         20         30         40         50         60 
MKSLVGVIMG STSDWETMKY ACDILDELNI PYEKKVVSAH RTPDYMFEYA ETARERGLKV 

        70         80         90        100        110        120 
IIAGAGGAAH LPGMVAAKTN LPVIGVPVQS KALNGLDSLL SIVQMPGGVP VATVAIGKAG 

       130        140        150        160 
STNAGLLAAQ ILGSFHDDIH DALELRREAI EKDVREGSEL V

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M. Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames EMBL AAP24324.1 and Ames / isolate Porton.
[2]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne EMBL AAT52606.1.
[3]	"Crystal structure of PurE (BA0288) from Bacillus anthracis at 1.8 A resolution." Boyle M.P., Kalliomaa A.K., Levdikov V., Blagova E., Fogg M.J., Brannigan J.A., Wilson K.S., Wilkinson A.J. Proteins 61:674-676(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
[4]	"The complete genome sequence of Bacillus anthracis Ames "Ancestor"." Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A. J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames Ancestor EMBL AAT29375.1 and Ames ancestor.
[5]	Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., Sutton G. Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Ames EMBL AAP24324.1.
[6]	"Elastic and inelastic diffraction changes upon variation of the relative humidity environment of PurE crystals." Oliete R., Pous J., Rodriguez-Puente S., Abad-Zapatero C., Guasch A. Acta Crystallogr. D 69:194-212(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP24324.1.
AE017334 Genomic DNA. Translation: AAT29375.1.
AE017225 Genomic DNA. Translation: AAT52606.1.

RefSeq

NP_842838.1. NC_003997.3.
YP_016900.1. NC_007530.2.
YP_026555.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XMP	X-ray	1.80	A/B/C/D/E/F/G/H	1-161	[»]
4AY3	X-ray	1.76	A/B/C/D	1-161	[»]
4AY4	X-ray	2.00	A/B/C/D	1-161	[»]
4B4K	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	1-161	[»]

SMR

Q81ZH8. Positions 2-161.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q81ZH8. 2 interactions.

STRING

198094.BA_0288.

Protocols and materials databases

DNASU

1085644.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAP24324; AAP24324; BA_0288.
AAT29375; AAT29375; GBAA_0288.
AAT52606; AAT52606; BAS0275.

GeneID

1085644.
2817097.
2851322.

KEGG

ban:BA_0288.
bar:GBAA_0288.
bat:BAS0275.

Phylogenomic databases

HOGENOM

HOG000034141.

K01588.

OMA

QSDWATM.

ProtClustDB

CLSK915770.

Enzyme and pathway databases

BioCyc

BANT260799:GJAJ-317-MONOMER.
BANT261594:GJ7F-326-MONOMER.

UniPathway

UPA00074; UER00943.

Family and domain databases

Gene3D

3.40.50.7700. 1 hit.

InterPro

IPR024694. N5-CAIR_mutase_PurE.
IPR000031. N5-CAIR_Mutase_PurE_dom.
[Graphical view]

Pfam

PF00731. AIRC. 1 hit.
[Graphical view]

PIRSF

PIRSF001338. AIR_carboxylase. 1 hit.

SMART

SM01001. AIRC. 1 hit.
[Graphical view]

SUPFAM

SSF52255. AIR_carboxyl. 1 hit.

TIGRFAMs

TIGR01162. purE. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q81ZH8.

Entry information

Entry name

Q81ZH8_BACAN

Accession

Primary (citable) accession number: Q81ZH8
Secondary accession number(s): E9RB02

Q6KY27

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information