PUR4_COLP3
ID PUR4_COLP3 Reviewed; 1320 AA.
AC Q47XX7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=CPS_3675;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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}.
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DR EMBL; CP000083; AAZ24314.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47XX7; -.
DR SMR; Q47XX7; -.
DR STRING; 167879.CPS_3675; -.
DR EnsemblBacteria; AAZ24314; AAZ24314; CPS_3675.
DR KEGG; cps:CPS_3675; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000547; 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..1320
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264571"
FT DOMAIN 1067..1320
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1160
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 310..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 687
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 726
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 730
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 894
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 896
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1320 AA; 144259 MW; B101D5EE17AD23F8 CRC64;
MIKNLRGAPA LSDFRVKKLL AQCEQLQLPV NDIYAEFAHF TKLNEELSTS EEKVLQQLLT
YGPTIEEHQP AGLFLLVTPR PGTISPWSSK STDIAHNCGL AKVERLERGI AYYVTLENDA
QLSTSQEAQL NTLLHDRMME SIFNDFAQAS TLFASSEPGE LTAIDIESGG KNALVQANIE
LGLALAEDEV NYLFENFTKL GRNPHDIELY MFAQANSEHC RHKIFNAEWT IDGVKQEKSL
FKMIRNTHEI NPDYVLSAYK DNAAVMVGNK GGRFFPNPET NVYGYNHEDI QILMKVETHN
HPTAISPYPG AATGSGGEIR DEGATGIGSK PKAGLVGFSV SNLRIPDFVQ PWETDFGKPS
RIVTAFDIMI EGPLGGAAFN NEFGRPAILG YFRTYEEEVN SFNGKEVRGY HKPIMLAGGL
GNIRDEHVQK REIIVGANLI ALGGPAMNIG LGGGAASSMA SGQSAESLDF ASVQRENPEM
ERRCQEVIDK CWQLGEENPI AFIHDVGAGG LSNAFPELVA DGGRGGIFEL RNVPNDERSM
APHEIWCNES QERYVIAVSD KNLATFEQIC QRERAPYSVV GRATEEEHLT VTDSHFSDNE
KLNTPIDLPL DVLLGKTPKI YKDVKTATAA GDSLDLSTVT LADAADRILS LPTVAEKTFL
ITIGDRSVTG MVNRDQMVGP WQVPVADCGV TASALDSYHG EAMSLGERTP VALLNFGASA
RLAVAESLTN IAGTDIGDLN RIKLSANWMS PAGHPGEDAG LYEAVKAIGE ELCPALGLTI
PVGKDSMSMK TQWEENGEQK SVTSPLSLVI TAFGVVEDIR KTVTPELRTD KGDTRLVAID
LSKGKKRLGG SCLAQVYKQL GSETPDVDDA EVLKGFFNAM QTLVRAEKVI AYHDISDGGL
FTTVTEMAFA GHTGVDIDIS KLSNGANDDL ATLFNEELGG VIQIRESDVD AIHAILAQHG
ILENCTDIGR LNNEDTIRFS RDGEVVLENS RTYYRTVWAQ TTYRMQSLRD NPECAQQEHD
VKFDTEDPGL NTELTFDINE DIVADLIIRD AVKDAENSAN DITNPRVAIL REQGVNSHVE
MAAAFDRAGF VAIDVHMSDI LSGRADLADF NGLVACGGFS YGDVLGAGEG WAKSILFNAN
ARTMFKTFFE REDTFTLGVC NGCQMLSNLK DIIPGSEHWP HFVQNKSERF EARFSLVEIQ
ESPSVLFKGM EGSRMPIAVS HGEGHAEFSS DAAIDAANNS GTVSMRYVNN YGDVTETYPA
NPNGSVDGIT SLTTTDGRVT IMMPHPERVF RTVANSWHPD SWGEDSPWVR MFRNARAFIG
