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Database: UniProt
Entry: C0QBX6_DESAH
LinkDB: C0QBX6_DESAH
Original site: C0QBX6_DESAH 
ID   C0QBX6_DESAH            Unreviewed;       509 AA.
AC   C0QBX6;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 98.
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=guaA1 {ECO:0000313|EMBL:ACN14988.1};
GN   Synonyms=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN   OrderedLocusNames=HRM2_18870 {ECO:0000313|EMBL:ACN14988.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14988.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN14988.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(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}.
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DR   EMBL; CP001087; ACN14988.1; -; Genomic_DNA.
DR   RefSeq; WP_015903774.1; NC_012108.1.
DR   AlphaFoldDB; C0QBX6; -.
DR   STRING; 177437.HRM2_18870; -.
DR   MEROPS; C26.957; -.
DR   KEGG; dat:HRM2_18870; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_7; -.
DR   OMA; DQLTCMF; -.
DR   OrthoDB; 9802219at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000442; 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:UP000000442}.
FT   DOMAIN          192..384
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         219..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   509 AA;  56571 MW;  DD6BAB8DB9FFE94D CRC64;
     MILIIDFGSQ FNQLIARRVR ENEIYCQVEP AGIDIERIKA LNPEGIILSG GPSSIYEDDS
     PKVDTEIFNL NVPILGICYG MQFMVNALGG SIERSDKREY GFADLTIKDH APLFTGLEKS
     TQVWMSHGDS TNRLPAGFTV TASTKNTEIA AMADNKNHFY GLQFHPEVEH TLGGFEMLKN
     FLFNVCHCEK SWTMSSFVTG AVEQIKEAVG DKKVIMGLSG GVDSSVAALL IHRAIGKNLY
     CIFVDNGLLR NNERTNLEKS LTTHLDMNIR FVDARRLFLD QLAGVEDPEK KRKIIGNLFI
     DVFEDEAKKI DGAEFLGQGT LYPDIIESKS AFGGPTSIIK SHHNVGGLPE KMKLKLVEPL
     QFLFKDEVRK LGLELGLNEN LVWRQPFPGP GLAIRIMGAV SEKRLSILKA ADTLLLEEIR
     AAGLYRKLWQ SFAVLLPIKS VGVMGDKRTY DSCIAIRAVT SKDAMTADWA RLPHELLATV
     SNRIINEVDG VNRVVFDITS KPPGTIEWE
//
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