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Database: UniProt
Entry: R9HTZ4_BACUN
LinkDB: R9HTZ4_BACUN
Original site: R9HTZ4_BACUN 
ID   R9HTZ4_BACUN            Unreviewed;      1234 AA.
AC   R9HTZ4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ORFNames=C801_02010 {ECO:0000313|EMBL:EOS07497.1};
OS   Bacteroides uniformis dnLKV2.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1235787 {ECO:0000313|EMBL:EOS07497.1, ECO:0000313|Proteomes:UP000014212};
RN   [1] {ECO:0000313|EMBL:EOS07497.1, ECO:0000313|Proteomes:UP000014212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=dnLKV2 {ECO:0000313|Proteomes:UP000014212};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides uniformis dnLKV2.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00004920, ECO:0000256|HAMAP-Rule:MF_00419}.
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 family.
CC       {ECO:0000256|ARBA:ARBA00008608, ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOS07497.1}.
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DR   EMBL; ASSO01000008; EOS07497.1; -; Genomic_DNA.
DR   RefSeq; WP_016273183.1; NZ_KE159486.1.
DR   AlphaFoldDB; R9HTZ4; -.
DR   PATRIC; fig|1235787.3.peg.2036; -.
DR   HOGENOM; CLU_001031_0_2_10; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000014212; Unassembled WGS sequence.
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   CDD; cd01740; GATase1_FGAR_AT; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF18076; FGAR-AT_N; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR   SUPFAM; SSF82697; PurS-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00419}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00419};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00419};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00419};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00419};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00419};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00419}; Reference proteome {ECO:0000313|Proteomes:UP000014212}.
FT   DOMAIN          14..80
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          122..171
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          380..533
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          781..907
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1079
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1192
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1194
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         624
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         663
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         667
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         828
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         830
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1234 AA;  136517 MW;  3463C5BFDCC9C1CF CRC64;
     MILFFRTPSK SVIAVECNHE LPQADSDKLC WLFGEATPES EDNLKGHFVG PRREMITPWS
     TNAVEITQNM GLDGIIRIEE YFPVKDENAD HDPMLQRMYK GLDQNVFTTN RQPEPIVHIE
     DLEAYNEKEG LALSKEEMDY LKKVEKDLGR PLTDSEVFGF AQINSEHCRH KIFGGTFIID
     GVEQESSLFQ MIKKTTQENP NKIISAYKDN VAFAEGPVIE QFAPADHSKP DYFQVKDIKS
     VISLKAETHN FPTTVEPFNG ASTGTGGEIR DRMGGGKGSW PIAGTAVYMT SYPRTEEGRP
     WEEILPVRKW LYQTPEQILI KASNGASDFG NKFGQPLICG SVLTFEHKEK DEVYGYDKVI
     MLAGGVGYGT QRDCLKGTPE AGNKVVVIGG DNYRIGLGGG SVSSVDTGRY SSGIELNAVQ
     RANAEMQKRA YNVVRALCEE ETNPVVSIHD HGSAGHVNCL SELVEECGGL IDMSKLPIGD
     TTLSAKEIIA NESQERMGLL IQEEAIEHVR KVAERERAPM YVVGETTGDH RFAFQQADGV
     RPFDLAVEQM FGSSPKTYMV DKTVERHYEM PQYELSQLHE YLTNVLQLEA VACKDWLTNK
     VDRSVTGKIA RQQCQGELQL PLSDCGVVAL DYRGEKGIAT SLGHAPQAAL ADPAAGSVLS
     VSEALTNLVW APLAEGLDSV SLSANWMWPC RSQEGEDARL YTAVKALSDF CCSLQINVPT
     GKDSLSMTQK YPDGSKVISP GTVIVSAGGE VSDVKKVVSP VLVNNEKTTI YHIDFSFDNL
     KLGGSAFAQT LGKVGDEVPS VQDAEYFRDA FLAVQELVNK GLILAGHDIS AGGLITTLLE
     MCFANVEGGM EINLDKIKEQ DLIKILFAEN PGIVIQVSDK HKEAVKQILE DAGVGYVKLG
     KPTDERHILV SKGDATYQFG IDYMRDVWYS TSYLLDRKQS MNGSAKKRFE NYKMQPVEFA
     FMPDFKGKFS QYGIDPDRRT PSGIRAAIIR EKGTNGEREM AYSLYLAGFD VKDVTMTDLI
     SGRETLEDVN MIVYCGGFSN SDVLGSAKGW AGAFLFNPKA KEALDKYYAR EDTLSLGVCN
     GCQLMMELNL INPEHKKNGK MLHNDSHKFE SRFLGVTVPT NRSVMLGSLS GSKLGIWVAH
     GEGKFSLPYD EDKYNVVLKY SYDEYPSNPN GSDYSIAGLA SADGRHLAMM PHLERAIFPW
     QNGCYPADRV NSDQITPWVE AFVNARKWVE ANKK
//
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