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Database: UniProt
Entry: A0A1A0UFJ8_9MYCO
LinkDB: A0A1A0UFJ8_9MYCO
Original site: A0A1A0UFJ8_9MYCO 
ID   A0A1A0UFJ8_9MYCO        Unreviewed;       364 AA.
AC   A0A1A0UFJ8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367, ECO:0000256|HAMAP-Rule:MF_00741};
DE            EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047, ECO:0000256|HAMAP-Rule:MF_00741};
DE   AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931, ECO:0000256|HAMAP-Rule:MF_00741};
DE   AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093, ECO:0000256|HAMAP-Rule:MF_00741};
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908, ECO:0000256|HAMAP-Rule:MF_00741};
GN   Name=purM {ECO:0000256|HAMAP-Rule:MF_00741};
GN   ORFNames=A5758_03025 {ECO:0000313|EMBL:OBB69790.1};
OS   Mycobacterium sp. 852014-50255_SCH5639931.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB69790.1, ECO:0000313|Proteomes:UP000092113};
RN   [1] {ECO:0000313|EMBL:OBB69790.1, ECO:0000313|Proteomes:UP000092113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB69790.1,
RC   ECO:0000313|Proteomes:UP000092113};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC         ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00023392, ECO:0000256|HAMAP-
CC         Rule:MF_00741};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004686, ECO:0000256|HAMAP-Rule:MF_00741}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741}.
CC   -!- SIMILARITY: Belongs to the AIR synthase family.
CC       {ECO:0000256|ARBA:ARBA00010280, ECO:0000256|HAMAP-Rule:MF_00741}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBB69790.1}.
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DR   EMBL; LZSV01000002; OBB69790.1; -; Genomic_DNA.
DR   RefSeq; WP_067735227.1; NZ_LZSV01000002.1.
DR   AlphaFoldDB; A0A1A0UFJ8; -.
DR   STRING; 1834112.A5758_03025; -.
DR   OrthoDB; 9777881at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000092113; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02196; PurM; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR   HAMAP; MF_00741; AIRS; 1.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR004733; PurM_cligase.
DR   NCBIfam; TIGR00878; purM; 1.
DR   PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR   PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00741}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00741};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00741}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00741}.
FT   DOMAIN          70..174
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          186..352
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   364 AA;  38419 MW;  4054709A97FF3C50 CRC64;
     MTDPGKSPGR SPGTHGITYA SAGVDIEAGD RAVEMFKPLA TKATRPEVRG GLGGFAGLFA
     LRNDYREPLL AASTDGVGTK LAVAQAMDKH DTVGLDLVAM VVDDLVVCGA EPLFLQDYIA
     VGRTVPERLS AIVAGIAEGC VRAGCALLGG ETAEHPGLME PDHYDISATG IGVVEADDVL
     GPERVKPGDT IIAMGSSGLH SNGYSLARTV LLEIDRMNLA GYVEEFGRTL GEELLEPTRI
     YAKDCLALTA ETHVRTFCHV TGGGLAGNLQ RVIPHGLVAE IDRGTWTPAP VFAMIAQRGR
     VAREEMEKTF NMGVGMVAIV APEDTDRALA ILTARHLDCW VLGTVCKGGK EGPRAKLVGQ
     HPRF
//
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