ID Q5SLC6_THET8 Unreviewed; 333 AA.
AC Q5SLC6;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 127.
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 OrderedLocusNames=TTHA0367 {ECO:0000313|EMBL:BAD70190.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70190.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0000313|EMBL:BAD70190.1, ECO:0000313|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:5AVM}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RX PubMed=26515187; DOI=10.1093/jb/mvv107;
RA Kanagawa M., Baba S., Watanabe Y., Nakagawa N., Ebihara A., Kuramitsu S.,
RA Yokoyama S., Sampei G.I., Kawai G.;
RT "Crystal structures and ligand binding of PurM proteins from Thermus
RT thermophilus and Geobacillus kaustophilus.";
RL J. Biochem. 159:313-321(2016).
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; AP008226; BAD70190.1; -; Genomic_DNA.
DR RefSeq; WP_011227884.1; NC_006461.1.
DR RefSeq; YP_143633.1; NC_006461.1.
DR PDB; 5AVM; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-333.
DR PDBsum; 5AVM; -.
DR AlphaFoldDB; Q5SLC6; -.
DR SMR; Q5SLC6; -.
DR EnsemblBacteria; BAD70190; BAD70190; BAD70190.
DR GeneID; 3169103; -.
DR KEGG; ttj:TTHA0367; -.
DR PATRIC; fig|300852.9.peg.367; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_0; -.
DR PhylomeDB; Q5SLC6; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5AVM};
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:UP000000532}.
FT DOMAIN 53..160
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 172..332
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 333 AA; 35404 MW; 3E3A706809C99F6D CRC64;
MRYEEAGVHI EAKAEALRRA REAIAATYTP EVLRGMGAFG GLYAASRLKA LEEPVLVATT
DGVGTKTLLA LEAGDVSGLG FDLVNHSVND LLAQGAEPLF FLDYLAASHL DEGVLAALLA
SLAEACRAHG IPLLGGETAE MPGVYREGAW DIAGTLVGVV ERSRILGPER VREGDALLAL
PSSGPHTNGY SLIRKVVAGQ DLSAPVPELG ESLKEALLRP HRAYLKEFRL LWEAGVELHA
AAHITGGGLP ENLPRALPPG LGAEVRRGSW PIPPVFPYLQ RLGGIPEEEM YRVFNMGLGM
VLVLPQEAAE EALKLVEGFL VGRVVPGEGV RLV
//