PUR4_HAEIN
ID PUR4_HAEIN Reviewed; 1297 AA.
AC P43847;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
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=HI_0752;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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=AAC22411.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC22411.1; ALT_INIT; Genomic_DNA.
DR PIR; H64090; H64090.
DR RefSeq; NP_438911.1; NC_000907.1.
DR RefSeq; WP_032828325.1; NC_000907.1.
DR AlphaFoldDB; P43847; -.
DR SMR; P43847; -.
DR STRING; 71421.HI_0752; -.
DR EnsemblBacteria; AAC22411; AAC22411; HI_0752.
DR KEGG; hin:HI_0752; -.
DR PATRIC; fig|71421.8.peg.790; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR PhylomeDB; P43847; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000579; 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; Reference proteome.
FT CHAIN 1..1297
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100409"
FT DOMAIN 1045..1297
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 301..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; 142747 MW; DCD23A9DA666E393 CRC64;
MTVKTFRGSP ALSEFRLTQL QQKCQQYQLP ITSVYAEYLH FVEQKTSLVE DEIVKLQALL
HYGSMFSELK PAGYCLIVTP RVGTISSWSS KATDIAHNCG LSKVNRIERG IAYYFNIERD
LTEAELATLK DLLHDRMLET VLNHETEAAL LFTQQEPKAL TTIDILNGGR QALEQANIAL
GLALADDEMD YLVESFTALK RNPQDVELYM FAQANSEHCR HKIFNADWII DGKKQDKSLF
KMIKNTFEQT PDFVLSAYKD NAAVMEGSKV GRWFPDPDGQ YRVHQEDVHI LMKVETHNHP
TAISPFPGAA TGSGGEIRDE GATGRGAKPK AGLTGFSVSN LVIPNFEQPW ENPLSKPNRI
ASALDIMIDA PLGSAAFNNE FGRPALLGYF RTYEEKVNSF AGKEVRGYHK PIMLAGGIGN
IRGEQVQKGE IPIGAKLIVL GGAAMNIGLG GGAASSMDSG KSKEDLDFAS VQRENPEMER
RCQEVIDRCW QLGEENPILF IHDVGAGGLS NAMPELVHDG KRGGKFDLRS ILCDEKGMSP
LEIWCNESQE RYVLAVAPEN LELFTALCER ERAPFAVIGE ATQAEHLILH DSHFDNNPID
LPMNVLLGKT PKMTREVLSK TVENQSLKIE SIQLKEAFHR VLRLPVVAEK TFLITIGDRS
VTGMVARDQM VGPWQIPVSD VAVTTASLDS YHGEAMAIGE RSPVALLDFS ASARLAVAEA
ITNIAGTLIG EMKRIKLSAN WMSAAGHTGE DAGLYEAVKA VGEELCPALG LTIPVGKDSM
SMKTTWIDNG EQKSVTAPLS LVISAFARVE DVRKTLTPQL RTDKGFSSLL LIDLGEGHNR
LGATALAQVY KQLGDKPADV VKVQRLKDFY NAMQTLVAED KLLAYHDRSD GGLITTLAEM
AFAGHCGVEV DISALGDNDL AVLFNEELGA VIQVADSQLE SVREVLKAHN LLGIIHQLGT
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 NGSSEGITAI TNLDGRVAIM
MPHPERVFRA VSNSWHPENW TEDGAWMRLF RNARMVF
