GUAA_THET8
ID GUAA_THET8 Reviewed; 503 AA.
AC Q5SI28;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=TTHA1552;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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.
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC Rule:MF_00344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008226; BAD71375.1; -; Genomic_DNA.
DR RefSeq; WP_011228757.1; NC_006461.1.
DR RefSeq; YP_144818.1; NC_006461.1.
DR PDB; 2YWB; X-ray; 2.10 A; A/B/C/D=1-503.
DR PDB; 2YWC; X-ray; 2.20 A; A/B/C/D=1-503.
DR PDBsum; 2YWB; -.
DR PDBsum; 2YWC; -.
DR AlphaFoldDB; Q5SI28; -.
DR SMR; Q5SI28; -.
DR STRING; 300852.55772934; -.
DR MEROPS; C26.A07; -.
DR EnsemblBacteria; BAD71375; BAD71375; BAD71375.
DR GeneID; 3168703; -.
DR KEGG; ttj:TTHA1552; -.
DR PATRIC; fig|300852.9.peg.1523; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_0; -.
DR OMA; KRKIIGH; -.
DR PhylomeDB; Q5SI28; -.
DR UniPathway; UPA00189; UER00296.
DR EvolutionaryTrace; Q5SI28; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00344; GMP_synthase; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR022955; GMP_synthase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glutamine amidotransferase; GMP biosynthesis;
KW Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..503
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000229481"
FT DOMAIN 1..189
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 190..378
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 217..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:2YWB"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:2YWB"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 284..306
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2YWB"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 396..415
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 422..431
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 446..454
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:2YWB"
FT HELIX 468..481
FT /evidence="ECO:0007829|PDB:2YWB"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:2YWB"
SQ SEQUENCE 503 AA; 55817 MW; 05525201070DF58F CRC64;
MVLVLDFGSQ YTRLIARRLR ELRAFSLILP GDAPLEEVLK HRPQALILSG GPRSVFDPDA
PRPDPRLFSS GLPLLGICYG MQLLAQELGG RVERAGRAEY GKALLTRHEG PLFRGLEGEV
QVWMSHQDAV TAPPPGWRVV AETEENPVAA IASPDGRAYG VQFHPEVAHT PKGMQILENF
LELAGVKRDW TPEHVLEELL REVRERAGKD RVLLAVSGGV DSSTLALLLA KAGVDHLAVF
VDHGLLRLGE REEVEGALRA LGVNLLVVDA KERFLKALKG VEDPEEKRKI IGREFVAAFS
QVARERGPFR FLAQGTLYPD VIESAGGHGA AKIKSHHNVG GLPEDLEFEL LEPFRLLFKD
EVRELALLLG LPDTLRLRHP FPGPGLAVRV LGEVTEERLE ILRRADDIFT SLLREWGLYE
KVAQALAVLT PVRSVGVAGD ERKYGYVLAL RAVTTEDFMT ADWARLPLEF LDEAARRITR
RVPEIGRVVY DLTSKPPATI EWE
