ID GUAA_HELHP Reviewed; 1375 AA.
AC Q7VG78;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=Probable GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=guaA; OrderedLocusNames=HH_1444;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE017125; AAP78041.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VG78; -.
DR SMR; Q7VG78; -.
DR STRING; 235279.HH_1444; -.
DR KEGG; hhe:HH_1444; -.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_255986_0_0_7; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002495; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:InterPro.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01997; GMP_synthase_C; 1.
DR CDD; cd04301; NAT_SF; 2.
DR Gene3D; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.880; -; 2.
DR Gene3D; 3.40.630.30; -; 3.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR005019; Adenine_glyco.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00884; guaA_Cterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF13673; Acetyltransf_10; 2.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR Pfam; PF03352; Adenine_glyco; 1.
DR Pfam; PF00117; GATase; 2.
DR Pfam; PF00958; GMP_synt_C; 1.
DR PRINTS; PR00099; CPSGATASE.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 3.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 2.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 2.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
DR PROSITE; PS51186; GNAT; 3.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..1375
FT /note="Probable GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140132"
FT DOMAIN 7..119
FT /note="Glutamine amidotransferase type-1; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 141..300
FT /note="N-acetyltransferase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 318..484
FT /note="N-acetyltransferase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 501..580
FT /note="Glutamine amidotransferase type-1; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 612..765
FT /note="N-acetyltransferase 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 1055..1250
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT REGION 120..500
FT /note="Insert-1"
FT REGION 597..1071
FT /note="Insert-2"
FT REGION 1011..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 1083..1089
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 1375 AA; 154160 MW; AB9A95D23FB8C636 CRC64;
MQENNVQILV LDFGSQYTQL IARRLREYGV YTEIVPYFEK LDSIKSKNPK GIILSGGPAS
VYEKDAYKPD SAIFTLGIPI LGICYGMQLI AQHFGGRVIK ADAQEFGKAV LEIMESSQDS
KDSSCFAFQG ASQGIQAPMT LSFDIFSHHK FPQMLTALLD LWEDSVQASH IFLTKQHIAE
IRLEVKAALQ SSQNIITATD KKDFLGFIGV EKNKIEMLFV ASSVFRKGIG KALLKEALER
YLKDYPYILV DCNEQNTQGL AFYKSLGFEK VGMSEKDSAG RDFPIVHLKV SKAILKKALE
RGTSDSVANA FVCESERVFL RPYTQADFAA LHKIVSDKET MYAWGQGFSK KQSQEWLDKQ
LAHYQQYGFG IWAIIEKQSG AIIGNAGLNH TEISLKGKTQ KIVEIGYLLH RDFWGKGYGS
EVARMCVKYG FETLGLEEVY CLIKEDNTAS IKVAKRLEMQ KVGEYPKPYK GKKISHLVFR
LEKKVWQESK NNATQGFKSC SLFKGIKQDS IVWMSHADKV ESIPQGFREL AKSGNTHYCA
IADSKRKIYA LQFHPEVVHS ECGGQMLQNF AVGICGANTC WNMRHFAQNE IEKLRRIVYG
GKAHCENPMS FMQIQEAFKH IGKAQTIQRL VEIWEEGARA THKDLSENEI AGMREEIREA
ILKSKNLLIA QKNEEWLGFI EIEKNEIAML FVVPKAFRKG VGKALLKEAF MRYLGAFEVI
KVNSLEWALG FYQALGFAKT GKKPIPAGSA GAFSPELIPL SIARESLQKS LGLEAQDSNE
GVREKVRCAW ATDKDEAARK LYEDYHDTEW GEPLHEDKKL FEHLVLEGFQ AGLSWITILK
KREAFRVAFD DFDPHIVANY DEDKIKELMR NEGIIRNRAK IEAAIINAKA FMAVQREFGS
FDKYIWGFVG GKPIINAFES IADLPASTPL SDKIAKDLKK RGFKFVGTTT MYAMMQSIGM
VNDHLTSCFK CNSSLGMQCD KILDFSQGTN TKSANLTKNP KNLHSHTANT RIVDSQHTES
SDIKGQSHLE SSADSGSAVS LRDFKSCEGA TRGSYLEGND RSGVANSLKI TKETTSKVLC
AVSGGVDSSV VAALLYRAIG ENLIPVFVDT GLLRKGEREA VEKIFKENLK VPLITADASE
LFLSRLKGVL DPEIKRKIIG ETFIEVFEKE AKKHNTKGEI KFLAQGTLYP DVIESVSVKG
PSKTIKSHHN VGGLPEWMKF ELIEPLRELF KDEVRALGRE LGMPESMLMR HPFPGPGLAI
RIMGEVNKAD LDLLREADSI FIDELHKQSY YDKVWQAFCV LLNVRSVGVM GDNRTYDNTI
CVRAVEAIDG MTATFAHLPH DFLEGVSNRI INEVEGINRV VYDITSKPPG TIEWE
//
