ID A0A180FUZ6_9BACT Unreviewed; 1222 AA.
AC A0A180FUZ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ECO:0000313|EMBL:OAV76072.1};
GN ORFNames=Barb7_00275 {ECO:0000313|EMBL:OAV76072.1};
OS Bacteroidales bacterium Barb7.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1633203 {ECO:0000313|EMBL:OAV76072.1, ECO:0000313|Proteomes:UP000078281};
RN [1] {ECO:0000313|EMBL:OAV76072.1, ECO:0000313|Proteomes:UP000078281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barb7 {ECO:0000313|EMBL:OAV76072.1,
RC ECO:0000313|Proteomes:UP000078281};
RA Tai V., Carpenter K.J., Weber P.K., Nalepa C.A., Perlman S.J.,
RA Keeling P.J.;
RT "Genomic and NanoSIMS analyses of nitrogen-fixing bacterial ectosymbionts
RT of a protist inhabiting a wood-eating cockroach.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OAV76072.1}.
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DR EMBL; LBCZ01000015; OAV76072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180FUZ6; -.
DR PATRIC; fig|1633203.3.peg.913; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000078281; 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; cd01740; GATase1_FGAR_AT; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000078281}.
FT DOMAIN 13..80
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 123..171
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 381..532
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 774..897
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1069
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1182
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1184
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 619
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 658
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 662
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 822
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1222 AA; 133897 MW; C119362F96490E2A CRC64;
MIVFFRSSAK TVLAVEAAQA FSPEDMQKLV WLFNEATPVT AGTVDGWFAG PRREMITPWS
TNAVEIAQNM GLAGISRIEE YRPVASGDAA HDPMLQRLYD GLNQELFTIN KQPAPILYIE
DVEAYNRQEG LALSGEEVSY LKEVSRKLNR RLTDSEVYGF AQVNSEHCRH KIFNGVFIID
GEEQESSLFK LIRKTSEENP NRLVSAYTDN VAFNEGPSIE QFAPLSGDTP DYYAVKDIPT
VLSLKAETHN FPTTVEPFNG AATGTGGEIR DRLGGGKASQ PLAGTAVYMT AYPRTDGARA
WEKILDPRQW LYQTPEQILI KASNGASDFG NKFGQPLICG SLLTFEHMEN GKKYAYDKVI
MLAGGVGFAN RRDALKGNPE TGEKVVVLGG DNYRIGMGGG AVSSVDTGLF TSGIELNAVQ
RANPEMQKRA ANVIRAIAES DDNPIVSIHD HGAGGHLNCL SELVEATGGH IDMSRLPIGD
PTLSAKEIIG NESQERMGLL IREQDVERVR RIAERERAPM YVVGETTGDM RLVFDTAINL
PLEYMFGKPP KTVMTDRTLN EPHRSIVYKE SELYHYLENV LQLEAVACKD WLTNKVDRSI
TGKVARQQCQ GELQLPLSDL GAVALDYRGK AGIATSIGHA PQAAMIDSEA GSVLAIAEAL
TNIVFAPLTD KLSGVSLSAN WMWPCRNEGE DARLYKAVKA ASDFACALGI NIPTGKDSLS
MTQKYGSDKV IAPGTVIISA GAEVSDVRKI VPTAMLPQEG YLYYIDFSFD SFKLGGSAFA
QALNTLGDEV PTATDPEYFA DAFNAIQDAI EKGLLLAGHD ISAGGMITAL LEMCFANTAG
GLEVNLDNLA EKDIIKILFA ENPGILVQVK DQKPFEKLME AAGVGFAAIA RPTAERHILV
SKGNARYSFD IDALRDVWYK SSYLLDRKQS GNVCAADRFA NYKKQPLAFK YNKGFTGKLS
YYALSADRRT PSGIRAAVIR EKGSQCERET AYALYLAGFD VKDVHTTDLV SGRETLQDVN
FIVFCGGFSN SDVLGSAKGW AGGLLYNEKA KKAIDAYYAR KDTLSMGICN GCQLMAELEL
LYPEHDQKHK MLHNDSHKFE SGFVTLEIPE NNSVMFGSLS GTKLGAWVAH GEGKFSFPYD
ETAYSIIARY NYADYPANPN GSLRSVAGVC SHDGRHLAIM PHPERAIFPW QCGYYPADRS
ADEVTPWIEA FVNARKWVEN CR
//
