PUR4_MANSM
ID PUR4_MANSM Reviewed; 1297 AA.
AC Q65RJ7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=MS1806;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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:0000255|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:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00419}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000255|HAMAP-Rule:MF_00419}.
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DR EMBL; AE016827; AAU38413.1; -; Genomic_DNA.
DR RefSeq; WP_011200969.1; NC_006300.1.
DR AlphaFoldDB; Q65RJ7; -.
DR SMR; Q65RJ7; -.
DR STRING; 221988.MS1806; -.
DR PRIDE; Q65RJ7; -.
DR EnsemblBacteria; AAU38413; AAU38413; MS1806.
DR KEGG; msu:MS1806; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000607; Chromosome.
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-KW.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 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 Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..1297
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264579"
FT DOMAIN 1044..1297
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1137
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 307..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 679
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 886
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 888
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1297 AA; 142440 MW; 171374406217BEB4 CRC64;
MFQIFRGSPA LSEFRLNQLS ARFQKADLPV KSCYAEYLHF ADLSAGLSAE ETDELEQLLH
YGPTLAQHES KGECFVVIPR VGTISSWSSK ATDIAHNCGL DKVVRLERGI AYYFEFERTL
SAEQQQRLVS HIHDRMMETV VRAPEQAAVL FDSQDPKPFT TVDILNGGRK ALEIANVELG
LALASDEMDY LVENFTALGR NPNDIELYMF AQANSEHCRH KIFNADWVID GEKQEKSLFK
MIKNTFEKTP DHVLSAYKDN AAVMEGSKVG RFFADQDGQY RYHNEDAHIL MKVETHNHPT
AISPFPGAAT GSGGEIRDEG ATGRGAKPKA GLVGFSVSNL VIPGFEQPWE NELSKPSRIS
SALDIMIEGP LGGAAFNNEF GRPALLGYFR TYEEKVNSFA GEEVRGYHKP IMLAGGIGNI
RAEHVQKGEI PVGAKLIVLG GPAMNIGLGG GAASSMTSGK SKEDLDFASV QRDNPEMERR
CQEVIDRCWQ MGEGNPIAFI HDVGAGGLSN AMPELVHDGG RGGKFELRNI LCDERGMSPL
EIWCNESQER YVLAVAPENL AVFEELCQRE RAPYAIIGEA TEEEHLTLHD NHFDNNPIDL
PMSLLLGKTP KMTRDVKSTQ VNNSPVDQTN IELKEAFHRV LRLPVVAEKT FLITIGDRTV
TGMVARDQMV GPWQIPVSDV AVTTAALDTY HGEAMSIGER APVALLDFAA SARLAVAESI
TNIAATNIGD IKRIKLSANW MSAAGHEGED AGLYEAVKAV GEELCPALGL TVPVGKDSMS
MKTTWSENGE QKTVTAPLSL VISAFARVED VRKTVTPQLR TDKGETALLL IDLGEGKNRL
GATALAQVYK QLGDKPADVV NVELLKGFYN AMQTLVQQGK LLAYHDRSDG GLIVTLAEMA
FAGNCGIRAE ISALGDNDLG ILFSEELGAV IQVRESDLAA VREVLTQHGL IHLTKDLGLV
TEYDEFEIKR GTKVVLSEKR SELRGIWAEL THQMQRLRDN PECADQEFAA KKDPANQGFS
AHLTYDINED VAAPYIATGK KPRIAVLREQ GVNSHVEMGA AFDRAGFEAI DVHMSDLHTA
RQNLKDFNAL VACGGFSYGD VLGAGGGWAK SVLFNTALRD QFQAFFERED TLALGVCNGC
QMISTLADII PGTENWPRFV RNTSERFEAR AALVRINESN SVWFQGMAGS HMPIAVSHGE
GRVEFKNDSQ LQGLRDQGLI IAQYVDNNIR PTEVYPANPN GSVDGITALS NTNGRVAIMM
PHPERVFRTV SNSWHPEDWS EDGAWMRLFR NARVFFK
