ID A0A139BX84_9PROT Unreviewed; 332 AA.
AC A0A139BX84;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=AWT59_0182 {ECO:0000313|EMBL:KXS33624.1};
OS Candidatus Gallionella acididurans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Gallionella.
OX NCBI_TaxID=1796491 {ECO:0000313|EMBL:KXS33624.1, ECO:0000313|Proteomes:UP000070578};
RN [1] {ECO:0000313|EMBL:KXS33624.1, ECO:0000313|Proteomes:UP000070578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33624.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXS33624.1, ECO:0000313|Proteomes:UP000070578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33624.1};
RA Kadnikov V., Ivasenko D., Beletsky A., Mardanov A., Danilova E.,
RA Pimenov N., Karnachuk O., Ravin N.;
RT "New uncultured bacterium of the family Gallionellaceae from acid mine
RT drainage: description and reconstruction of genome based on metagenomic
RT analysis of microbial community.";
RL Submitted (MAR-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:KXS33624.1}.
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DR EMBL; LSLI01000003; KXS33624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139BX84; -.
DR PATRIC; fig|1796491.3.peg.197; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000070578; 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:UP000070578}.
FT DOMAIN 46..151
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 163..326
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 332 AA; 35174 MW; C2EBE8828FFA28AF CRC64;
MDIDAGDRLV ENIKPFAKRT MRPEVLGGIG GFGALVEISK KYREPVLVSG TDGVGTKLRL
AFELNRHDTV GIDLVGMSVN DILVQGAEPL FFLDYFACGK LDVDAATEVI KGIAFGCEQA
GCALIGGETA EMPGMYPAGE YDLAGFAVGV VEKSAIISGA DIRAGDTVIG LASNGAHSNG
YSLVRKIIST RKADLGQKLD GIPLADLIMA PTRIYVKPLL ALMKSLTVKG MAHITGGGLL
ENVPRVLPEN VVAQLDGKAW HTPALFDWLR EMGNVAPQEM YRTFNCGIGM VVIVAKQDAD
AAMAQLNAAG ERATIIGTIR ARQGNETQTQ VS
//
