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Database: UniProt
Entry: D2XU38_RHOBT
LinkDB: D2XU38_RHOBT
Original site: D2XU38_RHOBT 
ID   D2XU38_RHOBT            Unreviewed;       303 AA.
AC   D2XU38;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=GMP synthase {ECO:0000313|EMBL:ADB23124.1};
DE            EC=6.3.5.2 {ECO:0000313|EMBL:ADB23124.1};
DE   Flags: Fragment;
GN   Name=guaA {ECO:0000313|EMBL:ADB23124.1};
OS   Rhodopirellula baltica.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=265606 {ECO:0000313|EMBL:ADB23124.1};
RN   [1] {ECO:0000313|EMBL:ADB23124.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SH398 {ECO:0000313|EMBL:ADB23124.1};
RX   PubMed=19948850; DOI=10.1128/AEM.01525-09;
RA   Winkelmann N., Jaekel U., Meyer C., Serrano W., Rachel R.,
RA   Rossello-Mora R., Harder J.;
RT   "Determination of the diversity of Rhodopirellula isolates from European
RT   seas by multilocus sequence analysis.";
RL   Appl. Environ. Microbiol. 76:776-785(2010).
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DR   EMBL; GU255233; ADB23124.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2XU38; -.
DR   MEROPS; C26.957; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADB23124.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}.
FT   DOMAIN          137..303
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        23
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         164..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADB23124.1"
FT   NON_TER         303
FT                   /evidence="ECO:0000313|EMBL:ADB23124.1"
SQ   SEQUENCE   303 AA;  33311 MW;  4F1DE20B7251BE78 CRC64;
     YEEGAPKCDE GLFDLGIPVL GICYGMQLAC QALGGKVDNT PSREYGRAMC DFVDRDSIFR
     GMQESEQVWM SHGDQVSQIA DQFTAMAKTS TCPYAAIRHN ERPVFGMQFH PEVTHTPHGG
     QILRNFVIDV CGCDGSWKLG DFADAAIESI RKQVGDKRVI CGLSGGVDSS VVAALLYKAI
     GPQLSCILVD NGLLRKNEQQ IVLEEFSNHF KTDLHVVEAE DRFLADLAGI DEPQEKRRRI
     GHAFIECFKD EAARIEDAHF LAQGTLYPDV IESGADKDGP AATIKLHHNV GGLPEELGFE
     LIE
//
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