GUAAA_PYRHO
ID GUAAA_PYRHO Reviewed; 189 AA.
AC O59071;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000255|HAMAP-Rule:MF_01510};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_01510};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_01510};
GN Name=guaAA {ECO:0000255|HAMAP-Rule:MF_01510}; OrderedLocusNames=PH1346;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC Rule:MF_01510}.
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_01510};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01510}.
CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_01510}.
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DR EMBL; BA000001; BAA30452.1; -; Genomic_DNA.
DR PIR; D71006; D71006.
DR PDB; 1WL8; X-ray; 1.45 A; A=1-189.
DR PDB; 2D7J; X-ray; 1.89 A; A=1-189.
DR PDBsum; 1WL8; -.
DR PDBsum; 2D7J; -.
DR AlphaFoldDB; O59071; -.
DR SMR; O59071; -.
DR STRING; 70601.3257769; -.
DR MEROPS; C26.A31; -.
DR EnsemblBacteria; BAA30452; BAA30452; BAA30452.
DR KEGG; pho:PH1346; -.
DR eggNOG; arCOG00087; Archaea.
DR OMA; GPDMDRI; -.
DR BRENDA; 6.3.5.2; 5244.
DR UniPathway; UPA00189; UER00296.
DR EvolutionaryTrace; O59071; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01510; GMP_synthase_A; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR023686; GMP_synthase_A.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glutamine amidotransferase; GMP biosynthesis;
KW Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..189
FT /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT /id="PRO_0000140230"
FT DOMAIN 2..189
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 168
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1WL8"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1WL8"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1WL8"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:1WL8"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1WL8"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1WL8"
FT TURN 112..117
FT /evidence="ECO:0007829|PDB:2D7J"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:1WL8"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1WL8"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:1WL8"
SQ SEQUENCE 189 AA; 21517 MW; 560F55F7A4BB92A7 CRC64;
MMIVIMDNGG QYVHRIWRTL RYLGVETKII PNTTPLEEIK AMNPKGIIFS GGPSLENTGN
CEKVLEHYDE FNVPILGICL GHQLIAKFFG GKVGRGEKAE YSLVEIEIID EDEIFKGLPK
RLKVWESHMD EVKELPPKFK ILARSETCPI EAMKHEELPI YGVQFHPEVA HTEKGEEILR
NFAKLCGEL
