ID A0A0P7YXG4_9GAMM Unreviewed; 357 AA.
AC A0A0P7YXG4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, 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 ECO:0000313|EMBL:KPQ23956.1};
GN ORFNames=HLUCCA13_11440 {ECO:0000313|EMBL:KPQ23956.1};
OS Halomonas sp. HL-48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1479235 {ECO:0000313|EMBL:KPQ23956.1, ECO:0000313|Proteomes:UP000050569};
RN [1] {ECO:0000313|EMBL:KPQ23956.1, ECO:0000313|Proteomes:UP000050569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-48 {ECO:0000313|EMBL:KPQ23956.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPQ23956.1}.
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DR EMBL; LJZS01000013; KPQ23956.1; -; Genomic_DNA.
DR RefSeq; WP_027335893.1; NZ_LJZS01000013.1.
DR AlphaFoldDB; A0A0P7YXG4; -.
DR STRING; 1479235.GCA_000686925_00876; -.
DR PATRIC; fig|1479235.4.peg.143; -.
DR eggNOG; COG0150; Bacteria.
DR OrthoDB; 9777881at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000050569; 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}.
FT DOMAIN 68..172
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 185..351
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 357 AA; 37512 MW; 8D64917EAF236331 CRC64;
MTDTSPSRAS SAPSLSYKDA GVDIDAGNAL VDRIKHVAKR TTRPEVMGGL GGFGALCELP
QGYRQPVLVS GTDGVGTKLR LAMMLGKHDT IGIDLVAMCV NDLIVAGAEP LLFLDYYATG
KLNVDIAADV VTGIGAGCEQ AGCALVGGET AEMPGMYEGD DYDLAGFCVG VVEKSEILDG
SRVGEGDVLL GLASSGPHSN GYSLIRKIIE RSEAPLDTPI DGTALGDALM APTRIYVKAL
LSLLRDSGLS VHALSHITGG GLLENIPRVL PDSLAARIDT QAWSRPAVFD WLQTQGNVAD
TEMYRVLNCG IGMVVVVPEH EADQAKAHLE AQGETVYRLG QIEARQQDAV VLENLPA
//
