GUAAB_PYRHO
ID GUAAB_PYRHO Reviewed; 308 AA.
AC O59072;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
GN Name=guaAB; OrderedLocusNames=PH1347;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of the GMP synthase from Pyrococcus horikoshii OT3.";
RL Submitted (NOV-2006) to the PDB data bank.
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}.
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; BA000001; BAA30453.1; -; Genomic_DNA.
DR PIR; E71006; E71006.
DR RefSeq; WP_010885436.1; NC_000961.1.
DR PDB; 2DPL; X-ray; 1.43 A; A/B=1-308.
DR PDB; 3A4I; X-ray; 1.79 A; A/B=1-308.
DR PDBsum; 2DPL; -.
DR PDBsum; 3A4I; -.
DR AlphaFoldDB; O59072; -.
DR SMR; O59072; -.
DR STRING; 70601.3257770; -.
DR EnsemblBacteria; BAA30453; BAA30453; BAA30453.
DR GeneID; 1443673; -.
DR KEGG; pho:PH1347; -.
DR eggNOG; arCOG00085; Archaea.
DR OMA; EGGIKSH; -.
DR OrthoDB; 31932at2157; -.
DR BRENDA; 6.3.5.2; 5244.
DR UniPathway; UPA00189; UER00296.
DR EvolutionaryTrace; O59072; -.
DR Proteomes; UP000000752; 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 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; 2.
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.
FT CHAIN 1..308
FT /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT /id="PRO_0000140249"
FT DOMAIN 1..185
FT /note="GMPS ATP-PPase"
FT BINDING 28..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2DPL"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:2DPL"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 97..119
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2DPL"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 203..222
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 239..259
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:2DPL"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:2DPL"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:2DPL"
SQ SEQUENCE 308 AA; 34562 MW; 8B209770605AE4BA CRC64;
MDWGRFVEEK VREIRETVGD SKAIIALSGG VDSSTAAVLA HKAIGDRLHA VFVNTGFLRK
GEPEFVVKTF RDEFGMNLHY VDAQDRFFSA LKGVTDPEEK RKIIGRVFIE VFEEVAKKIG
AEYLIQGTIA PDWIESQGKI KSHHNVGGLP EKLNLKLIEP LRDLYKDEVR ELAKFLGLPE
KIYNRMPFPG PGLAVRVIGE VTPEKIRIVR EANAIVEEEV ERAGLRPWQA FAVLLGVKTV
GVQGDIRAYK ETIAVRIVES IDGMTANAMN VPWEVLQRIA FRITSEIPEV GRVLYDITNK
PPATIEFE
