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PUR4_IDILO
ID   PUR4_IDILO              Reviewed;        1295 AA.
AC   Q5QWY0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=IL0591;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(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; AE017340; AAV81432.1; -; Genomic_DNA.
DR   RefSeq; WP_011233847.1; NC_006512.1.
DR   AlphaFoldDB; Q5QWY0; -.
DR   SMR; Q5QWY0; -.
DR   STRING; 283942.IL0591; -.
DR   PRIDE; Q5QWY0; -.
DR   EnsemblBacteria; AAV81432; AAV81432; IL0591.
DR   KEGG; ilo:IL0591; -.
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; UP000001171; 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..1295
FT                   /note="Phosphoribosylformylglycinamidine synthase"
FT                   /id="PRO_0000264578"
FT   DOMAIN          1042..1295
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1260
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1262
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         305..316
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         384..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         676
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         677
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         716
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         720
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         884
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         886
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1295 AA;  142005 MW;  D08A563F6584A26F CRC64;
     MEIYRGAPAL SAFKTTKQLE QLKQAGIPVK ELYAEYQHFV DLHNELSDEH RSVLVQLLKY
     GPEMPAHEPQ GALVLVTPRI GTISPWASKA TDIAHNCGLK SIHRVERGVA FYLQGDLSAE
     ELKQAALLLH DRMTESVLYD MNDAQQLFRS QEPQPLSSVD ILAGGREALA QANISLGLAL
     ADDEIDYLVE NFRKLDRNPN DIELYMFAQA NSEHCRHKIF NADWTIDGAE QPKSLFKMIK
     NTFETTPDYV LSAYKDNAAV MEGHEAGRFY PQPDSMSYGY SHEPVHILMK VETHNHPTAI
     SPYPGAATGS GGEIRDEGAT GVGSKPKAGL VGFSVSNLNI PGFKQPWEEN YGKPARIVSA
     LDIMLEGPLG GAAFNNEFGR PALTGYFRTY EQTVDSHNGR ETRGYHKPIM IAGGLGNIRE
     AHVQKGDIPV GAKLVVLGGP AMNIGLGGGA ASSMASGEST EDLDFASVQR ENPEMERRCQ
     EVIDRCWQLG ADNPIAFIHD VGAGGLSNAM PELVSDGGRG GRFELREIPN DEPGMTPLEI
     WCNESQERYV IAIAPENLAR FEALCERERA EYAVIGEATE ELTILLNDAK FSNQPIDLSL
     DVLLGKPPKM HRDVARLQTE GTPLHLEAAD LNDAADRLLR LPAIAEKTFL ITIGDRSVTG
     LVARDQMVGP WQIPVADVAV TASSYDSYHG EAMAMGERTP LALLNFGASA RMAVAESLTN
     IAAADIGDLK RIKLSANWMC AAGHPGEDAG LYEAVKAVGE ELCPELGITI PVGKDSMSMK
     TQWQQDGEDK AVTAPMSLVI TAFGRVNDIR STLTPQLRTD KGQSHLVLID LGKGQNRLGG
     SALAQVYQQL GQHTPDLDDT ETFKAFFNTT QQLVTEGRLL AYHDRSDGGL FTTVAEMAFA
     GNCGAKVALD ELGEDNLATL FNEELGAVIQ VSDEQYQKVM DAYKTAGLGD CVKRIGEPTH
     EDAIVFTRDE QNVLAQSRTH WRTVWAETTH HMQRLRDNPV CADEEFRLKQ RADNPGLLAD
     LTFDPSEDIA APYIAKGVAP KVAILREQGV NSHYEMAAAF DRAGFEAVDV HMSDILAGRV
     SLEDMQALAA CGGFSYGDVL GAGEGWAKSI LFNDRAREQF EAFFKRNDTL ALGVCNGCQM
     LSTLKQLIPG TEHWPRFVTN RSERFEARFS LVEVQESKSI FLGDMAGSRM PIAVSHGEGR
     AEFANPQQQS QLEQNSQVAL RYIDNWGEVA EQYPANPNGS PKGITAVTSD DGRVTAMMPH
     PERVFRTVAN SWHPDEWGED SPWMRMFRNA RKHLG
 
 
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