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Database: UniProt
Entry: A0A1L7D1K2_9CORY
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ID   A0A1L7D1K2_9CORY        Unreviewed;       351 AA.
AC   A0A1L7D1K2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=CPHO_02465 {ECO:0000313|EMBL:APT91957.1};
OS   Corynebacterium phocae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161895 {ECO:0000313|EMBL:APT91957.1, ECO:0000313|Proteomes:UP000185491};
RN   [1] {ECO:0000313|EMBL:APT91957.1, ECO:0000313|Proteomes:UP000185491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M408/89/1 {ECO:0000313|EMBL:APT91957.1,
RC   ECO:0000313|Proteomes:UP000185491};
RA   Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT   44612(T)), isolated from the common seal (Phoca vitulina).";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009249; APT91957.1; -; Genomic_DNA.
DR   RefSeq; WP_075732925.1; NZ_VXKJ01000026.1.
DR   AlphaFoldDB; A0A1L7D1K2; -.
DR   STRING; 161895.CPHO_02465; -.
DR   KEGG; cpho:CPHO_02465; -.
DR   OrthoDB; 9777881at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000185491; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185491}.
FT   DOMAIN          56..160
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          172..336
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   351 AA;  36784 MW;  8EBE8C031A14EED7 CRC64;
     MTDNTYAAAG VSIEEGDRAV TLFAPHAKRA TRPEVMGGLG GFAGLFKLGK YNEPILAAGS
     DGVGTKLAVA QAMDKHDTIG IDLVAMCVDD LVVCGAEPLF LQDYIAVGKV VPEKVAEIVK
     GIAEGCVQAG CALLGGETAE HPGVMGADEY DVSATAVGVV EASELLGPDK VREGDILIAM
     GSSGLHSNGY SLARYVLLEQ AGLPLDGHVE ELGRTLGEEL LEPTRIYALD CLALANECEV
     STFCHVTGGG LAGNLARVIP EGLTAHVSRA TWTPGQIFKT ISSVGKVSLP EMEKTFNMGV
     GMIAIVSPED RDRAMAMLAA RHVDAWELGH ITKAQEADEA RVEMTGEHPN F
//
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