ID A0AA42CPV9_9HYPH Unreviewed; 530 AA.
AC A0AA42CPV9;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562, ECO:0000256|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746, 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 ECO:0000313|EMBL:MCW6510817.1};
GN ORFNames=M8523_22645 {ECO:0000313|EMBL:MCW6510817.1};
OS Lichenifustis flavocetrariae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Lichenihabitantaceae; Lichenifustis.
OX NCBI_TaxID=2949735 {ECO:0000313|EMBL:MCW6510817.1, ECO:0000313|Proteomes:UP001165667};
RN [1] {ECO:0000313|EMBL:MCW6510817.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BP6-180914 {ECO:0000313|EMBL:MCW6510817.1};
RA Pankratov T.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
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=XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP +
CC diphosphate + 2 H(+); 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MCW6510817.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAMOIM010000018; MCW6510817.1; -; Genomic_DNA.
DR RefSeq; WP_282587190.1; NZ_JAMOIM010000018.1.
DR AlphaFoldDB; A0AA42CPV9; -.
DR Proteomes; UP001165667; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR FunFam; 3.30.300.10:FF:000002; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.620:FF:000001; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.880:FF:000001; GMP synthase [glutamine-hydrolyzing]; 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 NCBIfam; NF000848; PRK00074.1; 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; 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:UP001165667}.
FT DOMAIN 213..405
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344"
FT ACT_SITE 186
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344"
FT ACT_SITE 188
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344"
FT BINDING 240..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 530 AA; 57621 MW; B8D4E436E6C66AF7 CRC64;
MQEQDESAVR AESQGHHHRV LIIDFGSQVT QLIARRVRDA GIYSEVVPFQ KASEAMAGSL
PDAFILSGGP ESVSQEGSPR APQAVFESGK PILGICYGQM AMAHQLGGEV NTGDHREFGR
ADLTIKGACA LFDDLWLDGQ SYPVWMSHGD AVTRMPEGFQ IVATSENAPC AVIADEARRY
YGLMFHPEVV HTPDGGRLIS NFLHKVVGLK SDWTMASFRD EALAQIRAQV GDGRVLCGLS
GGVDSAVAAV LIHEAIGEQL TCVFVDHGLL RQDEAKEVVT LFRDHYNIPL VHVDASDTFL
SALAGVTDPE TKRKTIGKLF IDVFEAEAAK IGGADFLAQG TLYPDVIESV SFSGGPSVTI
KSHHNVGGLP ERMNMKLVEP LRMLFKDEVR VLGRALGLPP AFVGRHPFPG PGLAIRIPGD
ITRGKLQILR QADAIYLEEI REAGLYDTIW QAFAVLLPVR TVGVMGDGRT YDQVCALRAV
TSVDGMTADF FPFDMAFIGR VATRIINEVK GINRVVYDVT SKPPGTIEWE
//
