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Database: UniProt
Entry: F0RLG1_DEIPM
LinkDB: F0RLG1_DEIPM
Original site: F0RLG1_DEIPM 
ID   F0RLG1_DEIPM            Unreviewed;       514 AA.
AC   F0RLG1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN   OrderedLocusNames=Deipr_0705 {ECO:0000313|EMBL:ADY25865.1};
OS   Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS   101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY25865.1, ECO:0000313|Proteomes:UP000007718};
RN   [1] {ECO:0000313|Proteomes:UP000007718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC   VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA   Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT   20540.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY25865.1, ECO:0000313|Proteomes:UP000007718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC   VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RX   PubMed=22768367; DOI=10.4056/sigs.2756060;
RA   Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA   Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA   Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the orange-red pigmented, radioresistant
RT   Deinococcus proteolyticus type strain (MRP(T)).";
RL   Stand. Genomic Sci. 6:240-250(2012).
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}.
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DR   EMBL; CP002536; ADY25865.1; -; Genomic_DNA.
DR   RefSeq; WP_013614474.1; NC_015161.1.
DR   AlphaFoldDB; F0RLG1; -.
DR   STRING; 693977.Deipr_0705; -.
DR   MEROPS; C26.957; -.
DR   KEGG; dpt:Deipr_0705; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_0; -.
DR   OMA; DQLTCMF; -.
DR   OrthoDB; 9802219at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000007718; 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; 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:UP000007718}.
FT   DOMAIN          199..389
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         227..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   514 AA;  56725 MW;  C080A5952ACB91F5 CRC64;
     MTQPSQHHQT VVILDFGSQF TRLIARRFRE MGAYSVILPG TAPLERIQQE QPVGIVLSGG
     PSSVYDENAP KPAPGVLDLN MPILGVCYGM QYLAHEAGGD VKRAGKREYG KADLTEYGGE
     LFKGIEGEFV AWMSHSDSVT QLPQGYQVVA KTEDTPVTAI ENNETKRYGV QFHPEVVHTP
     KGGQLLGNFL DICGVSRDWT PQHILDELIA GVQEQVGSEG RVLLGISGGV DSSTLALLLS
     RAVGDRLTAV FVDHGLLRLN EREQVETALR GAGVNVVTVD AREEFMHHLD GVSDPEQKRK
     IIGREFIRVF DRETEKYGPF EFLAQGTLYP DVIESAGGEG AANIKSHHNV GGLPEDLAFK
     LVEPFRTLFK DEVREIAKLL GLPDDIRMRH PFPGPGLAIR CLGAITEEKL DILRRVDDIF
     ISGLREFGLY DQCSQALAVL TPIQSVGVMG DERTYSYTVA LRAVTTGDFM TAEWARLPYE
     FLGTMSNRIV NQVHEVNRVV YDITGKPPAT IEWE
//
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