ID H3AFT5_LATCH Unreviewed; 683 AA.
AC H3AFT5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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:ENSLACP00000008506.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000008506.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000008506.2}
RP IDENTIFICATION.
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 EMBL; AFYH01007414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01007415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01007416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01007417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01007418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01007419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01007420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AFT5; -.
DR STRING; 7897.ENSLACP00000008506; -.
DR Ensembl; ENSLACT00000008574.2; ENSLACP00000008506.2; ENSLACG00000007529.2.
DR eggNOG; KOG1622; Eukaryota.
DR GeneTree; ENSGT00390000006591; -.
DR HOGENOM; CLU_014340_0_2_1; -.
DR InParanoid; H3AFT5; -.
DR OMA; DQLTCMF; -.
DR TreeFam; TF106132; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000007529; Expressed in pelvic fin and 6 other cell types or tissues.
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:UP000008672}.
FT DOMAIN 207..425
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 94
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 182
FT /evidence="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 683 AA; 75487 MW; 840F43C1DA19CC47 CRC64;
MAGGGGAKDG QRHYEGAIAI LDAGAQYGKV IDRRVREMFV QSEILPLETP AFAIKEQGFR
AIIISGGPSS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHR KNVREDGVFN
VGVDNTCSLF RGLQKEELVL LTHGDSVDKV ADGFKVVVQS GSIVAGIANE SKKLYGVQFH
PEVDLTEHGR EILKNFLFDI AGCSGTFTVQ NRELECIQEI KEKVGSSKVL VLLSGGVDST
VCTALLNKAL NRDQVIAVHI DNGFMRKRES QTVEEALKRL GIQVKVVNAA HAFYNGTTTL
PISDEDRTPR KRISKTLNMT TNPEEKRKII GDTFVNIANE VVGDMNLKPE EVFLAQGTLR
PDLIESASLL ASGKADVIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR ALGRELGLPE
ELVSRHPFPG PGLAIRVICA DEPFICKDFA ETSNILKIVA DFSASIKKPH TLLQRVKSCT
TEEEQEKLIQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPQW EALMFLARLI
PRMCHNINRL VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR ESGYAGKISQ
MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNQLPEE VVLKMVTEIK
KIPGISRVMY DLTSKPPGTT EWE
//