PUR4_HAEI8
ID PUR4_HAEI8 Reviewed; 1297 AA.
AC Q4QME6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=NTHI0909;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX87801.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000057; AAX87801.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005655525.1; NC_007146.2.
DR AlphaFoldDB; Q4QME6; -.
DR SMR; Q4QME6; -.
DR MEROPS; C56.972; -.
DR EnsemblBacteria; AAX87801; AAX87801; NTHI0909.
DR KEGG; hit:NTHI0909; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002525; 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_0000264575"
FT DOMAIN 1045..1297
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 303..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1138
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1263
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1265
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 308..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 680
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 887
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1297 AA; 142712 MW; A9479AC1DD005291 CRC64;
MTVKTFRGSP ALSEFRLTQL QQKCQQYQLP ITSVYAEYLH FVEQKTSLVE DEIVKLQALL
HYGSMFSELK PAGYCLIVTP RVGTISSWSS KATDIAHNCG LSKVNRIERG IAYYFNIERD
LTEAELATLK DLLHDRMLET VLNHETEAAL LFTQQEPKAL TTIDILNGGR QALERANIAL
GLALADDEMD YLVESFTALK RNPQDVELYM FAQANSEHCR HKIFNADWII DGKKQDKSLF
KMIKNTFEQT PDFVLSAYKD NAAVMEGSKV GRWFPDPDGQ YRVHQEDAHI LMKVETHNHP
TAISPFPGAA TGSGGEIRDE GATGRGAKPK AGLTGFSVSN LVIPNFEQPW ENPLSKPNRI
ASALDIMIDA PLGSAAFNNE FGRPALLGYF RTYEEKVNSF AGKEVRGYHK PIMLAGGIGN
IRGEQVQKGE IPIGAKLIVL GGAAMNIGLG GGAASSMDSG KSKEDLDFAS VQRENPEMER
RCQEVIDRCW QLGEENPILF IHDVGAGGLS NAMPELVHDG RRGGKFDLRS ILCDEKGMSP
LEIWCNESQE RYVLAVAPEN LELFTALCER ERAPFAVIGE ATQAEHLILH DSHFDNNPID
LPMNVLLGKT PKMTREVLSK TVENQSLKTE GIQLKEAFHR VLRLPVVAEK TFLITIGDRS
VTGMVARDQM VGPWQIPVSD VAVTTASLDS YHGEAMAMGE RSPVALLNFS ASARLAVAEA
ITNIAGTHIG EMKRIKLSAN WMSAAGHTGE DAGLYEAVKA VGEELCPALG LTIPVGKDSM
SMKTTWIDNG EQKSVTAPLS LVISAFARVE DVRKTLTPQL RTDKGLSSLL LIDLGEGHNR
LGATALAQVY KQLGDKPADV VKVQRLKDFY NAMQTLVAED KLLAYHDRSD GGLITTLAEM
AFAGHCGVEV DISALGDNDL AVLFNEELGA VIQVADSQLE SVREVLKAHN LLGITHQLGT
VTADDRFEIS RGSHKLFSEK RSELRSIWAE LTYQMQRLRD NPECAEQEFE AKKNPDDKGL
SAFLTYDVNE DITAPFINKG VKPTIAILRE QGVNSHYEMA AAFDRAGFNA IDVHMSDLMI
GRRNLAEFNA MVACGGFSYG DVLGAGGGWA KSILFNPKLH EQFSQFFINP NTLTLGVCNG
CQMISNLAEI IPGTENWPHF VRNKSERFEA RVSLVKINEV DSVWFAGMAG SHMPIAVSHG
EGQVKFKSVE QFAGLKAQGI IAAQYIDNNG SPTELYPANP NGSAEGITAI TNLDGRVAIM
MPHPERVFRA VSNSWHPENW TEDGAWMRLF RNARMVF
