PURQ_THEMA
ID PURQ_THEMA Reviewed; 213 AA.
AC Q9X0X2;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000255|HAMAP-Rule:MF_00421};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00421};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00421};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000255|HAMAP-Rule:MF_00421};
DE Short=FGAR amidotransferase I {ECO:0000255|HAMAP-Rule:MF_00421};
DE Short=FGAR-AT I {ECO:0000255|HAMAP-Rule:MF_00421};
DE AltName: Full=Glutaminase PurQ {ECO:0000255|HAMAP-Rule:MF_00421};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00421};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000255|HAMAP-Rule:MF_00421};
GN Name=purQ {ECO:0000255|HAMAP-Rule:MF_00421}; OrderedLocusNames=TM_1245;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), FUNCTION, ACTIVE SITE, AND SUBUNIT.
RX PubMed=18597481; DOI=10.1021/bi800329p;
RA Morar M., Hoskins A.A., Stubbe J., Ealick S.E.;
RT "Formylglycinamide ribonucleotide amidotransferase from Thermotoga
RT maritima: structural insights into complex formation.";
RL Biochemistry 47:7816-7830(2008).
CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC complex involved in the purines biosynthetic pathway. Catalyzes the
CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. The FGAM synthase complex is composed of three subunits.
CC PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC dependent manner. PurS interacts with PurQ and PurL and is thought to
CC assist in the transfer of the ammonia molecule from PurQ to PurL.
CC {ECO:0000255|HAMAP-Rule:MF_00421, ECO:0000269|PubMed:18597481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00421};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00421};
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 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00421}.
CC -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ
CC and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00421,
CC ECO:0000269|PubMed:18597481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00421}.
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DR EMBL; AE000512; AAD36320.1; -; Genomic_DNA.
DR PIR; G72276; G72276.
DR RefSeq; NP_229050.1; NC_000853.1.
DR RefSeq; WP_004080023.1; NZ_CP011107.1.
DR PDB; 3D54; X-ray; 3.50 A; D/H/L=1-213.
DR PDBsum; 3D54; -.
DR AlphaFoldDB; Q9X0X2; -.
DR SMR; Q9X0X2; -.
DR STRING; 243274.THEMA_08110; -.
DR DNASU; 898238; -.
DR EnsemblBacteria; AAD36320; AAD36320; TM_1245.
DR KEGG; tma:TM1245; -.
DR eggNOG; COG0047; Bacteria.
DR InParanoid; Q9X0X2; -.
DR OMA; LHFVCRD; -.
DR OrthoDB; 1527083at2; -.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; Q9X0X2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00421; PurQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01737; FGAM_synth_I; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Glutamine amidotransferase;
KW Hydrolase; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..213
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurQ"
FT /id="PRO_0000100598"
FT DOMAIN 5..213
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:18597481"
FT ACT_SITE 186
FT /evidence="ECO:0000305|PubMed:18597481"
FT ACT_SITE 188
FT /evidence="ECO:0000305|PubMed:18597481"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:3D54"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:3D54"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:3D54"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3D54"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:3D54"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3D54"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:3D54"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3D54"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:3D54"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:3D54"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:3D54"
SQ SEQUENCE 213 AA; 23588 MW; A68B5A2861B0698A CRC64;
MKPRACVVVY PGSNCDRDAY HALEINGFEP SYVGLDDKLD DYELIILPGG FSYGDYLRPG
AVAAREKIAF EIAKAAERGK LIMGICNGFQ ILIEMGLLKG ALLQNSSGKF ICKWVDLIVE
NNDTPFTNAF EKGEKIRIPI AHGFGRYVKI DDVNVVLRYV KDVNGSDERI AGVLNESGNV
FGLMPHPERA VEELIGGEDG KKVFQSILNY LKR
