A4YGQ3 (A4YGQ3_METS5) Unreviewed, UniProtKB/TrEMBL

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

Ordered Locus Names:

Msed_1448

Organism

Metallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]

Taxonomic identifier

399549 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Metallosphaera

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 ABP95605.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	5-(carboxyamino)imidazole ribonucleotide mutase activity Inferred from electronic annotation. Source: EC phosphoribosylaminoimidazole carboxylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A4YGQ3 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: A17568050D0F9B98	FASTA	157	16,884
	10 20 30 40 50 60 MPLVGVIMGS KSDWEVMKEA VDILKNFGVS YEVKVVSAHR TPEFMMKYAK EAHERGIEVI 70 80 90 100 110 120 IAGAGGAAHL PGMVASLTHL PVIGVPVPSR NLNGLDSLLS IVQMPYGVPV ATVAIGGAKN 130 140 150 AGLLAVRILS VKYPELGEKM RKFMEEMRND VLSTELV

References

[1]

"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism." Auernik K.S., Maezato Y., Blum P.H., Kelly R.M. Appl. Environ. Microbiol. 74:682-692(2008) [PubMed: 18083856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000682 Genomic DNA. Translation: ABP95605.1.
RefSeq	YP_001191529.1. NC_009440.1.
3D structure databases
ProteinModelPortal	A4YGQ3.
SMR	A4YGQ3. Positions 2-152.
ModBase	Search...
Protein-protein interaction databases
STRING	A4YGQ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5104818.
GenomeReviews	Gene locus Msed_1448 in contig CP000682_GR.
KEGG	mse:Msed_1448.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG10111.
HOGENOM	HBG301965.
OMA	LIMGSDS.
PhylomeDB	A4YGQ3.
ProtClustDB	CLSK802986.
Family and domain databases
InterPro	IPR024694. N5-CAIR_mutase_PurE. IPR000031. N5-CAIR_Mutase_PurE_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.7700. AIR_carboxyl. 1 hit.
KO	K01588.
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...

Entry information

Entry name

A4YGQ3_METS5

Accession

Primary (citable) accession number: A4YGQ3

Entry history

Integrated into UniProtKB/TrEMBL:	May 29, 2007
Last sequence update:	May 29, 2007
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)