(data stored in ACNUC7421 zone)

SWISSPROT: B4SJ80_STRM5

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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