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ID B4SJ80_STRM5 Unreviewed; 1294 AA.
AC B4SJ80;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 08-MAY-2019, entry version 84.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000256|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000256|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000256|HAMAP-Rule:MF_00419};
GN OrderedLocusNames=Smal_0543 {ECO:0000313|EMBL:ACF50248.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas;
OC Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50248.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF50248.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF50248.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in
CC the purines biosynthetic pathway. Catalyzes the ATP-dependent
CC conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. {ECO:0000256|HAMAP-Rule:MF_00419,
CC ECO:0000256|SAAS:SAAS00911929}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-D-
CC ribosyl)glycinamide = 2-(formamido)-N(1)-(5-phospho-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:58426, ChEBI:CHEBI:58478,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00419, ECO:0000256|SAAS:SAAS01143401};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000256|HAMAP-
CC Rule:MF_00419, ECO:0000256|SAAS:SAAS01143431}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS
CC family. {ECO:0000256|HAMAP-Rule:MF_00419,
CC ECO:0000256|SAAS:SAAS00911930}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00419}.
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DR EMBL; CP001111; ACF50248.1; -; Genomic_DNA.
DR STRING; 391008.Smal_0543; -.
DR MEROPS; C56.972; -.
DR EnsemblBacteria; ACF50248; ACF50248; Smal_0543.
DR KEGG; smt:Smal_0543; -.
DR eggNOG; ENOG4108ETH; Bacteria.
DR eggNOG; COG0046; LUCA.
DR eggNOG; COG0047; LUCA.
DR HOGENOM; HOG000261359; -.
DR KO; K01952; -.
DR OMA; SLSANWM; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001867; 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-UniRule.
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; IPR017926; GATASE.
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;
DR PRODOM; B4SJ80.
DR SWISS-2DPAGE; B4SJ80.
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00419,
KW ECO:0000256|SAAS:SAAS01143413};
KW Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419};
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419,
KW ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00911931};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00419,
KW ECO:0000256|SAAS:SAAS01143366, ECO:0000313|EMBL:ACF50248.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00419,
KW ECO:0000256|SAAS:SAAS01143383};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00419,
KW ECO:0000256|SAAS:SAAS01143388};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00419,
KW ECO:0000256|SAAS:SAAS01143406};
KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00419,
KW ECO:0000256|SAAS:SAAS01143445}.
FT DOMAIN 1045 1294 Glutamine amidotransferase type-1.
FT {ECO:0000259|PROSITE:PS51273}.
FT NP_BIND 300 311 ATP. {ECO:0000256|HAMAP-Rule:MF_00419}.
FT ACT_SITE 1138 1138 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_00419, ECO:0000256|PROSITE-ProRule:
FT PRU00605}.
FT ACT_SITE 1259 1259 {ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605}.
FT ACT_SITE 1261 1261 {ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605}.
FT METAL 675 675 Magnesium. {ECO:0000256|HAMAP-Rule:
FT MF_00419}.
FT METAL 714 714 Magnesium. {ECO:0000256|HAMAP-Rule:
FT MF_00419}.
FT METAL 718 718 Magnesium. {ECO:0000256|HAMAP-Rule:
FT MF_00419}.
FT METAL 887 887 Magnesium. {ECO:0000256|HAMAP-Rule:
FT MF_00419}.
FT BINDING 674 674 ATP; via carbonyl oxygen.
FT {ECO:0000256|HAMAP-Rule:MF_00419}.
FT BINDING 889 889 ATP. {ECO:0000256|HAMAP-Rule:MF_00419}.
SQ SEQUENCE 1294 AA; 139052 MW; E772529D46AE063E CRC64;
MMVLEGAPAL SPFRRERLES RLQSIAPSLR ISGAWHVYFV QPEGSAVPDL TTLCRILEAA
PQAEAVAEGA VSRIVVPRLG TLSPWSSKAT ELVRGAGQPV SRVERGLRID VQGWPADAAA
QQALIKALHD PMTQSVLENV EQGQALFSTP ARGELERVPV DQLEAANQRL GLAMAQDEID
YLRERFSALG RSPSDVELMM FAQANSEHCR HKIFNASWTI DGQEQDRSLF RMIKNTHQQT
PQHTLSAYSD NAAVIEGHPA SRYRPDPASG EYRSEPSVPS AFQIKVETHN HPTAIAPFPG
ASTGAGGEIR DEGATGRGGK PKAGLSGFSV SHLRIPELPQ PWEAPRALNP RMAPALEIMT
DGPLGGAAFN NEFGRPALLG YFRSFELPEG ADLVRAYDKP IMLAGGLGAI DRVQVDKILL
QDGDAVIVLG GPAMLIGLGG GAASSVASGE SAEDLDFASV QRDNPEMERR CQEVIDRCVA
MGADNPIKFF HDVGAGGLSN AIPELLHDSK VGGIIDLGKV PTDDPSLSPM QLWCNESQER
YVLGVAQERL AEFAALCARE RCPFAAVGVA TAEEHLVVAY GAVPGNIPAD APIDLPMDVL
FGKPPKMHRD TAHPPAPRWP ALKTGGLDLQ EAGLRVLAHP TVASKNFLVT IGDRSVGGLT
AREQMVGPWQ LPVADVAITL ADFNGVAGEA MALGERTPLA LLDAAASARM AVGEALTNLC
AAPVDALDEI KLSANWMAAA GHPGEDALLY DAVKAVGMEL CPQLDISIPV GKDSLSMQAQ
WHDQGEAHKS VSPVSLVITA FAPVADVRQQ LTPLLDREVE SELWLIGLGA GKQRLGGSIL
AQVHADHGDL PAFAGAAPDL DDPQRLRGFF ELIRDARQSG LLLAYHDRSD GGAFAALCEM
AFTSRLGLDI TLDAWGDDPF RSLFNEELGA VVQIAREDRA AFADLVERHA LTECAQRIAK
PTTAPVVRVS LGGENLAEWR WDALFDAWWS VTHAMQKRRD NPANADAERE IARAFTAPGL
KPKLSFDLNE DVAAPFISTG ARPRVAVLRE QGVNGQIEMA NIFERAGFRA FDVHMSDLIE
GRVALQDFTG LVACGGFSYG DVLGAGRGWA TSILERSALR DAFAAFFARE DSFALGVCNG
CQMMSQLKGI IPGAEHWPQF RRNASEQFEA RTALLEVVES PSILLRGMAG SRLQVAVAHG
EGQAVFDNAV DQAAARVSLR YIDGNGNVAS QYPLNPNGSP DGITGLTSTD GRVTIMMPHP
ERTPRALNMS WAPAEWQGDS PWMRMFRNAR VWCG
//
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