ID J7M2F4_STRP1 Unreviewed; 203 AA.
AC J7M2F4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 2.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
GN Name=purE {ECO:0000256|HAMAP-Rule:MF_01929,
GN ECO:0000313|EMBL:BAM29409.2};
GN ORFNames=M1GAS476_0052 {ECO:0000313|EMBL:BAM29409.2};
OS Streptococcus pyogenes M1 476.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1207470 {ECO:0000313|EMBL:BAM29409.2, ECO:0000313|Proteomes:UP000005248};
RN [1] {ECO:0000313|EMBL:BAM29409.2, ECO:0000313|Proteomes:UP000005248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=476 {ECO:0000313|Proteomes:UP000005248};
RX PubMed=22965090; DOI=10.1128/JB.01265-12;
RA Miyoshi-Akiyama T., Watanabe S., Kirikae T.;
RT "Complete Genome Sequence of Streptococcus pyogenes M1 476, Isolated from a
RT Patient with Streptococcal Toxic Shock Syndrome.";
RL J. Bacteriol. 194:5466-5466(2012).
CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC (CAIR). {ECO:0000256|HAMAP-Rule:MF_01929}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate;
CC Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730,
CC ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01929};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC {ECO:0000256|HAMAP-Rule:MF_01929}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01929}.
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DR EMBL; AP012491; BAM29409.2; -; Genomic_DNA.
DR AlphaFoldDB; J7M2F4; -.
DR KEGG; spym:M1GAS476_0052; -.
DR HOGENOM; CLU_094982_2_1_9; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000005248; Chromosome 1.
DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1970; -; 1.
DR HAMAP; MF_01929; PurE_classI; 1.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR NCBIfam; TIGR01162; purE; 1.
DR PANTHER; PTHR23046:SF2; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR PANTHER; PTHR23046; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT; 1.
DR Pfam; PF00731; AIRC; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01929};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01929}.
FT DOMAIN 44..195
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
SQ SEQUENCE 203 AA; 22037 MW; 06E9A7A5D02D74D3 CRC64;
MLKHLVALTW VRLRNQRFRT YLIFFYGKFR QVETPLCILI MKTPIISIIM GSKSDWATMQ
KTAEVLDNFG IAYEKKVVSA HRTPDLMFKH AEEARGRGIK IIIAGAGGAA HLPGMVAAKT
TLPVIGVPVK SRALSGLDLL YSIVQMPGGV PVATMAIGEA GATNAALTAL RILSIEDQNL
ADALAHFHEE QGKIAEESSG ELI
//
