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Database: UniProt
Entry: A0A1Q6WKA7_9GAMM
LinkDB: A0A1Q6WKA7_9GAMM
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ID   A0A1Q6WKA7_9GAMM        Unreviewed;      1299 AA.
AC   A0A1Q6WKA7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAMS {ECO:0000256|HAMAP-Rule:MF_00419};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00419};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAR amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAR-AT {ECO:0000256|HAMAP-Rule:MF_00419};
GN   Name=purL {ECO:0000256|HAMAP-Rule:MF_00419};
GN   ORFNames=AUH10_06195 {ECO:0000313|EMBL:OLB13515.1};
OS   Gammaproteobacteria bacterium 13_2_20CM_66_19.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1805166 {ECO:0000313|EMBL:OLB13515.1, ECO:0000313|Proteomes:UP000186999};
RN   [1] {ECO:0000313|EMBL:OLB13515.1, ECO:0000313|Proteomes:UP000186999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC       purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC       formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC       formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC         ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC         ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00419};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00004920, ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC       {ECO:0000256|ARBA:ARBA00008608, ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00419}.
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:OLB13515.1}.
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DR   EMBL; MNCZ01000057; OLB13515.1; -; Genomic_DNA.
DR   STRING; 1805166.AUH10_06195; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000186999; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR   HAMAP; MF_00419; PurL_1; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR040707; FGAR-AT_N.
DR   InterPro; IPR010073; PurL_large.
DR   InterPro; IPR041609; PurL_linker.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR036604; PurS-like_sf.
DR   NCBIfam; TIGR01735; FGAM_synt; 1.
DR   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF18076; FGAR-AT_N; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR   SUPFAM; SSF82697; PurS-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00419}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00419};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00419};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00419};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00419};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00419};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00419}.
FT   DOMAIN          35..154
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          174..223
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          434..592
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          842..956
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          305..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1139
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1264
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1266
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         310..321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         682
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         721
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         725
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         889
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         891
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1299 AA;  139842 MW;  FCF40239F1202717 CRC64;
     MLGIAGTAAL SPFRRPKLLE RLRAIEPAVT ALDSRFMHFV ECTRALTAGE RAVLLALLTY
     GPRPQAPPPA GEGAANRVLV VPRAGTISPW SSKATDIARV CGLEPVRRIE RGIEYRLEAP
     RPLGAARLEA LAPALFDRMT EMALLDASEV ARLFAHAAPR PLERVPLAAG RAALVEADRA
     RGLALSAEEI DYLLEIFARL RRDPSDVELM MFAQANSEHC RHKIFNARWI IDGEPREESL
     FAMIRYTHER SPAGVLSAYR DNAAVIEGSL GERYFPDPDT GIYRASAEPI DILMKVETHN
     HPTAISPFPG ASTGSGGEIR DEGATGRGAK PKAGLTGFSV SHLRIPGYER AWEGEFGAPA
     RIASPLDIMI EAPIGAASFN NEFGRPAVCG YFRTFEQRAA GDPPQRTRGY HKPIMIAGGL
     GNVRRAHVEK AAVEVGAKLV VLGGPAMLIG LGGGAASSLG SGSSSAELDF ASVQRGNAEM
     QRRAQEVIDR CWALGEDNPI ALIHDVGAGG LSNAVPEAVA HSRRGARVDL RAIPSAETGM
     SPMELWCNEA QERYVLAIPA ASLPRFAAIA ERERCPFAVI GEFDASGELV VRDPLFDEVP
     VDMPLAALLG EPPRLTREVR SVRVARAPFD TSRVALREAA YRVLRLPAVA DKTFLITIGD
     RTVGGLISRD QLVGRWQVAV SDVAVTLADY RGSAGEALAM GERTPVAVLD GPASGRLAVA
     EAITNILAAD IGPLSNIRLS ANWMAACGEA GEDAALYETV RAVGRELCPA LGIAIPVGKD
     SLSMRTVWSE GGVERRVVAP VSLIVSAFAP VADVRRTLTP ALELDERPSS LWLIDLARGR
     HRLGASALAQ VYGELGEEPA DLDEPSVLLR FAAALAELHA AGMLRAYHDR SDGGLFATLL
     EMAFAGHCGL DIALPSGRGP ALAQLFAEEP GVVVQILAQD EPRLESMLAR HGLADAALYL
     GAPVSELRVR MRIGTQEFDE SWADLRRAWS ETSWRMRRLR DDPECADEEF AAETAAADPG
     LSVALRFDPE EDIAAPYVSR GVRPALAILR EQGVNSQTET AAVCERAGFA AHDVHMTDLL
     GGRRSLGEFQ GLIACGGFSY GDVLGAGEGW AKSILFHESL REEFQRFFAR SDRFALGICN
     GCQMFAALRA IIPGTEHWPR FQRNRSEQYE ARFSLVEVLP SPSVVLDGMA GSILPVAVAH
     GEGRAEFESA AAAEACASSG LVGFRYVTHD CRVATTYPAN PSGSPFGLAA LTNTDGRVTI
     TMPHPERSVR YVQNSWRPRE SGEWSGWMRL FRNARRFAG
//
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