GUAAB_METJA
ID GUAAB_METJA Reviewed; 310 AA.
AC Q58531;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
GN Name=guaAB; OrderedLocusNames=MJ1131;
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:0000250}.
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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC (A) and a GMP-binding subunit (B). {ECO:0000305}.
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DR EMBL; L77117; AAB99133.1; -; Genomic_DNA.
DR PIR; B64441; B64441.
DR RefSeq; WP_010870642.1; NC_000909.1.
DR PDB; 6JP9; X-ray; 2.10 A; A/B/C/D=1-310.
DR PDBsum; 6JP9; -.
DR AlphaFoldDB; Q58531; -.
DR SMR; Q58531; -.
DR STRING; 243232.MJ_1131; -.
DR EnsemblBacteria; AAB99133; AAB99133; MJ_1131.
DR GeneID; 1452027; -.
DR KEGG; mja:MJ_1131; -.
DR eggNOG; arCOG00085; Archaea.
DR HOGENOM; CLU_014340_0_0_2; -.
DR InParanoid; Q58531; -.
DR OMA; EGGIKSH; -.
DR OrthoDB; 31932at2157; -.
DR PhylomeDB; Q58531; -.
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-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00345; GMP_synthase_B; 1.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR026598; GMP_synthase_B.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; GMP biosynthesis; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..310
FT /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT /id="PRO_0000140241"
FT DOMAIN 2..185
FT /note="GMPS ATP-PPase"
FT BINDING 29..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:6JP9"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 98..119
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6JP9"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 203..222
FT /evidence="ECO:0007829|PDB:6JP9"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 230..243
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 250..264
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6JP9"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:6JP9"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:6JP9"
SQ SEQUENCE 310 AA; 34806 MW; 77F966F92FC62B12 CRC64;
MFDPKKFIDE AVEEIKQQIS DRKAIIALSG GVDSSVAAVL THKAIGDKLT AVFVDTGLMR
KGEREEVEKT FRDKLGLNLI VVDAKDRFLN ALKGVTDPEE KRKIIGKLFI DVFEEIAEDI
KAEVLVQGTI APDWIETQGK IKSHHNVALP HGMVLEVVEP LRELYKDEVR LLAKELGLPD
SIVYRQPFPG PGLAVRVLGE VTEEKLNICR EANAIVEEEV KKANLDKDLW QYFAVVLDCK
ATGVKGDERE YNWIVALRMV KSLDAMTAHV PEIPFDLLKR ISKRITSEIP NVARVVFDIT
DKPPATIEFE
