ID F1MC86_BOVIN Unreviewed; 693 AA.
AC F1MC86;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN Name=GMPS {ECO:0000313|Ensembl:ENSBTAP00000017301.5,
GN ECO:0000313|VGNC:VGNC:29443};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000017301.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017301.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017301.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000017301.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017301.5};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
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DR AlphaFoldDB; F1MC86; -.
DR Ensembl; ENSBTAT00000017301.5; ENSBTAP00000017301.5; ENSBTAG00000013013.5.
DR VEuPathDB; HostDB:ENSBTAG00000013013; -.
DR VGNC; VGNC:29443; GMPS.
DR eggNOG; KOG1622; Eukaryota.
DR GeneTree; ENSGT00390000006591; -.
DR HOGENOM; CLU_014340_0_2_1; -.
DR TreeFam; TF106132; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000013013; Expressed in spermatid and 107 other cell types or tissues.
DR ExpressionAtlas; F1MC86; baseline and differential.
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; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; 2.
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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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}; Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 217..435
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 244..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 693 AA; 76582 MW; 7A9946FFDE3CF51E CRC64;
MALCNGDSKL ENAGGDLKDG HHHNEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK
KSVREDGVFS ISVDNTCSLF RGLQKEEIVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE
SKKLYGAQFH PEVGLTENGK VILKNFLYDI AGCSGTFTVQ NREIECIREI KEGVGTSKVL
VLLSGGVDST VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALRKL GIQVKVINAA
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMNLKPE
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR
ILGRELGLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW
ESLIFLARLI PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNEIPVE
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
//