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).
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; 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
//