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Database: UniProt
Entry: A3JPA7_9RHOB
LinkDB: A3JPA7_9RHOB
Original site: A3JPA7_9RHOB 
ID   A3JPA7_9RHOB            Unreviewed;       363 AA.
AC   A3JPA7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
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=RB2150_03838 {ECO:0000313|EMBL:EBA03597.1};
OS   Rhodobacteraceae bacterium HTCC2150.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA03597.1, ECO:0000313|Proteomes:UP000004731};
RN   [1] {ECO:0000313|EMBL:EBA03597.1, ECO:0000313|Proteomes:UP000004731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA03597.1,
RC   ECO:0000313|Proteomes:UP000004731};
RX   PubMed=20889754; DOI=10.1128/JB.01088-10;
RA   Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT   the Roseobacter clade.";
RL   J. Bacteriol. 192:6315-6316(2010).
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:EBA03597.1}.
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DR   EMBL; AAXZ01000002; EBA03597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3JPA7; -.
DR   eggNOG; COG0150; Bacteria.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000004731; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004731}.
FT   DOMAIN          77..180
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          192..356
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   363 AA;  37364 MW;  056D248CCBAAC69D CRC64;
     MVVIKQAQLN ISECAMSANK SPLTYAAAGV DIDAGNALVD RIKPAAASTK RSGVMSGLGG
     FGALFDLKGA GFTDPILVGA TDGVGTKLRI AIDTGNFDTI GVDLVAMCVN DLVCQGAEPL
     FFLDYFATGK LEIEAAATII EGIAAGCKAS GCALIGGETA EMPGMYHGGD FDLAGFSVGA
     MERGAHLPAD VQVGDVLLGL ASNGVHSNGY SLVRRIVERS GLSWDDPAPF GTESLGTHLL
     APTRLYVTQC LAAIRAGGVH ALAHITGGGL TENIPRVLPD GMGVAVDLSA WDLPPVFKWL
     VEVAELEQSE LLKTFNAGVG MVLAVDAVRA DDLVTLLQGE GETVLRLGHV TDTPGVAYSG
     KLV
//
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