UniProt: A0A1H0T2J0

Database: UniProt
Entry: A0A1H0T2J0_9MICO

LinkDB:  A0A1H0T2J0_9MICO 
Original site:  A0A1H0T2J0_9MICO

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (5)   
   Pfam (2)   
All databases (16)   

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ID   A0A1H0T2J0_9MICO        Unreviewed;       371 AA.
AC   A0A1H0T2J0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   18-JUN-2025, entry version 32.
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=SAMN04489867_2595 {ECO:0000313|EMBL:SDP47776.1};
OS   Pedococcus dokdonensis.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Intrasporangiaceae; Pedococcus.
OX   NCBI_TaxID=443156 {ECO:0000313|EMBL:SDP47776.1, ECO:0000313|Proteomes:UP000199077};
RN   [1] {ECO:0000313|Proteomes:UP000199077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22329 {ECO:0000313|Proteomes:UP000199077};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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 + phosphate +
CC         H(+); Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287,
CC         ChEBI:CHEBI:456216; EC=6.3.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00049057, 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|ARBA:ARBA00004496,
CC       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; LT629711; SDP47776.1; -; Genomic_DNA.
DR   RefSeq; WP_091786157.1; NZ_LT629711.1.
DR   AlphaFoldDB; A0A1H0T2J0; -.
DR   STRING; 443156.SAMN04489867_2595; -.
DR   OrthoDB; 9777881at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000199077; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:TreeGrafter.
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   GO; GO:0046084; P:adenine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd02196; PurM; 1.
DR   FunFam; 3.30.1330.10:FF:000001; Phosphoribosylformylglycinamidine cyclo-ligase; 1.
DR   FunFam; 3.90.650.10:FF:000011; Phosphoribosylformylglycinamidine cyclo-ligase; 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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00741}; Reference proteome {ECO:0000313|Proteomes:UP000199077}.
FT   DOMAIN          48..164
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          177..342
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   371 AA;  38226 MW;  02BF4DE67DCD241B CRC64;
     MSEPITYASA GVDVEAGDKA VELMKASVRR ATRPEVLGGL GGFAGMFDAA AIARMTHPVL
     ATSTDGVGTK VAIAQALDKH DTIGFDLVGM VVDDIVVCGA EPLFMTDYIA TGKVVPERIA
     AIVTGIAAAC EQARVALVGG ETAEHPGLLE PDEYDVAGAA TGVVEYADVL GPDRVVPGDV
     VLALGSSGLH SNGYSLVRKV IGAAGWDLDR DVQEFGQTLG EELLTPTRVY SADLLDLIRT
     DGIDVHALSH VTGGGLVANL ARVLPPTVFA RLDRASWTPP AVFSTIGRLG QVPRADLERT
     LNMGVGFVAM LPADQVDAAT RELAARGIPA WALGEVSAAE DAVVDTAHEV VRGAKGVEGG
     GVQLVGDHPA S
//

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