GenomeNet

Database: UniProt
Entry: A4ADE5_9GAMM
LinkDB: A4ADE5_9GAMM
Original site: A4ADE5_9GAMM 
ID   A4ADE5_9GAMM            Unreviewed;       524 AA.
AC   A4ADE5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562, ECO:0000256|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746, ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356, ECO:0000256|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN   ORFNames=KT71_18107 {ECO:0000313|EMBL:EAQ95943.1};
OS   Congregibacter litoralis KT71.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Congregibacter.
OX   NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ95943.1, ECO:0000313|Proteomes:UP000019205};
RN   [1] {ECO:0000313|EMBL:EAQ95943.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ95943.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA   Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA   Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT   "Characterization of a marine gammaproteobacterium capable of aerobic
RT   anoxygenic photosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN   [2] {ECO:0000313|EMBL:EAQ95943.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ95943.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA   Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT   "The photosynthetic apparatus and its regulation in the aerobic
RT   gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL   PLoS ONE 4:E4866-E4866(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000256|ARBA:ARBA00002332, ECO:0000256|HAMAP-Rule:MF_00344}.
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:0000256|HAMAP-Rule:MF_00344};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153, ECO:0000256|HAMAP-
CC       Rule:MF_00344}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00344}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAQ95943.1}.
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; AAOA02000001; EAQ95943.1; -; Genomic_DNA.
DR   RefSeq; WP_008296063.1; NZ_CM002299.1.
DR   AlphaFoldDB; A4ADE5; -.
DR   STRING; 314285.KT71_18107; -.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_6; -.
DR   OrthoDB; 9802219at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000019205; Chromosome.
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   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.30.300.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00344; GMP_synthase; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR022955; GMP_synthase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   NCBIfam; TIGR00888; guaA_Nterm; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00344};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00344};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW   Rule:MF_00344};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00344};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00344};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00344}; Reference proteome {ECO:0000313|Proteomes:UP000019205}.
FT   DOMAIN          207..399
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         234..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   524 AA;  57753 MW;  6CF1F3D042F134B3 CRC64;
     MTDIHASRIL ILDFGSQYTQ LIARRVREVG VYSEIRAWDI SEEELREFAP SGVILSGGPE
     SVTEEGSPRA PACLFEGNWP LLGICYGMQT MAAQLGGEVQ GSDTSEFGYA QIRTAGETAL
     LHDIRDHMTD HGDGLLDVWM SHGDKVTALP KDFSCVASTD SCPIAAMAHG SQPWFGIQFH
     PEVTHTLQGT RILERFVIEI CGCEALWTPA RIVEDAIARV RETVGGDHVL LGLSGGVDSS
     VVAALLHKAI GDQLTCVFVD NGLLRLHEGD QVMEMFARNM GVKVIRSDSE ALFLDRLAGV
     SDPEEKRKII GNTFIEVFDE EAAKIEGVRW LAQGTIYPDV IESAGAKTGK AHVIKSHHNV
     GGLPEDMALE LVEPLRELFK DEVRKIGLEL GLPHDMVFRH PFPGPGLGVR ILGEVKHAYA
     EILRRADAIY IEELRAAGWY EKTSQAFAVF LPVKSVGVVG DARRYEYVIA LRAVETVDFM
     TARWAHLPYE LLEKVSNRII NEITGVSRVT YDVSSKPPAT IEWE
//
DBGET integrated database retrieval system