GUAAA_METJA
ID GUAAA_METJA Reviewed; 188 AA.
AC Q58970;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 125.
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=MJ1575;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB99597.1; -; Genomic_DNA.
DR PIR; F64496; F64496.
DR RefSeq; WP_010871100.1; NC_000909.1.
DR PDB; 2LXN; NMR; -; A=1-188.
DR PDB; 7D40; X-ray; 1.67 A; A/B=1-188.
DR PDB; 7D95; X-ray; 1.67 A; A/B=1-188.
DR PDB; 7D96; X-ray; 2.29 A; A=1-188.
DR PDB; 7D97; X-ray; 1.89 A; A/B/C/D=1-188.
DR PDBsum; 2LXN; -.
DR PDBsum; 7D40; -.
DR PDBsum; 7D95; -.
DR PDBsum; 7D96; -.
DR PDBsum; 7D97; -.
DR AlphaFoldDB; Q58970; -.
DR BMRB; Q58970; -.
DR SMR; Q58970; -.
DR STRING; 243232.MJ_1575; -.
DR MEROPS; C26.A31; -.
DR EnsemblBacteria; AAB99597; AAB99597; MJ_1575.
DR GeneID; 1452484; -.
DR KEGG; mja:MJ_1575; -.
DR eggNOG; arCOG00087; Archaea.
DR HOGENOM; CLU_014340_1_4_2; -.
DR InParanoid; Q58970; -.
DR OMA; GPDMDRI; -.
DR OrthoDB; 79931at2157; -.
DR PhylomeDB; Q58970; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..188
FT /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT /id="PRO_0000140221"
FT DOMAIN 1..188
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:7D40"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2LXN"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:7D40"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:7D40"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7D40"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7D97"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:7D40"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7D97"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2LXN"
FT STRAND 148..162
FT /evidence="ECO:0007829|PDB:7D40"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2LXN"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:7D40"
SQ SEQUENCE 188 AA; 21020 MW; 3F1DDB0FA1F2D850 CRC64;
MIVILDNGGQ YVHRIHRSLK YIGVSSKIVP NTTPLEEIES NKEVKGIILS GGPDIEKAKN
CIDIALNAKL PILGICLGHQ LIALAYGGEV GRAEAEEYAL TKVYVDKEND LFKNVPREFN
AWASHKDEVK KVPEGFEILA HSDICQVEAM KHKTKPIYGV QFHPEVAHTE YGNEILKNFC
KVCGYKFE
