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Database: UniProt
Entry: V9VQP7_9RHOB
LinkDB: V9VQP7_9RHOB
Original site: V9VQP7_9RHOB 
ID   V9VQP7_9RHOB            Unreviewed;       348 AA.
AC   V9VQP7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=METH_10575 {ECO:0000313|EMBL:AHD01071.1};
OS   Leisingera methylohalidivorans DSM 14336.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD01071.1, ECO:0000313|Proteomes:UP000018780};
RN   [1] {ECO:0000313|EMBL:AHD01071.1, ECO:0000313|Proteomes:UP000018780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD01071.1,
RC   ECO:0000313|Proteomes:UP000018780};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (SEP-2013) 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; CP006773; AHD01071.1; -; Genomic_DNA.
DR   RefSeq; WP_024090363.1; NC_023135.1.
DR   AlphaFoldDB; V9VQP7; -.
DR   STRING; 999552.METH_10575; -.
DR   KEGG; lmd:METH_10575; -.
DR   PATRIC; fig|999552.6.peg.2115; -.
DR   HOGENOM; CLU_047116_0_0_5; -.
DR   OrthoDB; 9777881at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000018780; 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}.
FT   DOMAIN          62..166
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   348 AA;  35787 MW;  45A7A64EC6F933F8 CRC64;
     MTSGKNGLTY ADAGVDIDAG NALVDRIKPA AKRTNRSGVM SGLGGFGALF DLKAAGYNDP
     ILVGATDGVG TKLRIAIDTG VVDGVGIDLV AMCVNDLVCQ GAEPLFFLDY FATGKLETET
     AARIIEGIAE GCVRSGCALI GGETAEMPGM YPQGDFDLAG FAVGAMERGT ALPEGVQEGD
     VLLGLASDGV HSNGYSLVRK LVDVSGLGWD AECPFGEGTL GEALLTPTRL YVKQSLAAVR
     AGGVHALAHI TGGGLTENLP RVLPEGLGAD IDLNAWQLPG VFQWMAATGD IAEAEMLKTF
     NCGIGMILSV SADRADALIE LLEGEGETVS RLGTVTAGEG MRYTGNLL
//
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