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Database: UniProt
Entry: C6Y2G1_PEDHD
LinkDB: C6Y2G1_PEDHD
Original site: C6Y2G1_PEDHD 
ID   C6Y2G1_PEDHD            Unreviewed;      1222 AA.
AC   C6Y2G1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 80.
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=Phep_2973 {ECO:0000313|EMBL:ACU05171.1};
OS   Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS   / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU05171.1, ECO:0000313|Proteomes:UP000000852};
RN   [1] {ECO:0000313|EMBL:ACU05171.1, ECO:0000313|Proteomes:UP000000852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC   NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC   {ECO:0000313|Proteomes:UP000000852};
RX   PubMed=21304637; DOI=10.4056/sigs.22138;
RA   Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA   Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT   3).";
RL   Stand. Genomic Sci. 1:54-62(2009).
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}.
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DR   EMBL; CP001681; ACU05171.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6Y2G1; -.
DR   STRING; 485917.Phep_2973; -.
DR   KEGG; phe:Phep_2973; -.
DR   eggNOG; COG0046; Bacteria.
DR   eggNOG; COG0047; Bacteria.
DR   HOGENOM; CLU_001031_0_2_10; -.
DR   OMA; LSANWMW; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000000852; 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   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:UP000000852}.
FT   DOMAIN          11..89
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          381..533
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          779..897
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1069
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1182
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1184
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         260..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         664
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         668
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         826
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1222 AA;  134228 MW;  13699432B591F31C CRC64;
     MIYFFSSQSK TVFALQIERN LSTTDITKLE WLFGGAKLQQ ETTLNDFFVG PRAAMVTPWS
     TNAVEITQNM DIHGIIRIEE FQQVEENFSD YDPMLSQKYS KLDQDIYTIH IKPEPILQIS
     DIAAYNKQEG LSLSDEEIAY LNELSGRLGR ELTDSEVFGF SQVNSEHCRH KIFNGKFVID
     GIEQPISLFK LIRKTSEENP NDIVSAYKDN VAFIKGPKVQ QFAPKRADEP DYYTLSDFES
     VISVKAETHN FPTTVEPFNG AATGSGGEIR DRLAGGQGSL PLAGTAVYMT ALSRLEENRP
     WEKGVEERQW LYQTPMDILI KASNGATDFG NKFGQPLITG SVLTFEHEEN NRKLGFDKVI
     MLAGGVGYGK ASQAQKHKPA EGDKIVILGG ENYRIGMGGA AVSSADTGAL GTGIELNAVQ
     RSNPEMQKRA ANAVRGMVES DQNNIISIHD HGAGGHLNCL SELVEETGGK IDLDKLPVGD
     PTLSAKEIIG NESQERMGLV IGQEHINTLQ KIADRERSPM YTVGTVTGDH RFTFESASTG
     VKPMDLELKD MFGSSPKVVM EDKTIDRKYL PVTYDAAQLN TYLEQVLQLE AVACKDWLTN
     KVDRCVGGRV AKQQCAGPLQ LPLNNCGVMA LDFQGKEGIA TSVGHAPLSA LIDAGAGSRI
     AIAESLSNIV WAPLKDGLKS VSLSANWMWA CKNEGEDARL YEAVKACSDF AISLGINIPT
     GKDSLSMKQK YKDGDVIAPG TVIISAAGNC NDITRVVEPV LQKNGGAIYY INLSNDTYKL
     GGSSFAQILN RIGNETPDVK DAATFKKTFD ILQQLIKEGK IQAGHDIGSG GLITTLLEMC
     FADRDLGASL DLSALGEQDI IKLLFAENIG IVFQADATVE ASFAANGIAL HKIGELSTAA
     TLTIKNGSAE SLNFDVDQLR DVWFKTSYLL DKKQSGPVKA KERFDNYKHQ VLKYNFPAHF
     DGKKPVIDAS KPRPKAAIIR EKGSNSEREL ANAMYLAGFD VKDVHMTDLI TGRETLEDIQ
     FIGAVGGFSN SDVLGSAKGW AGAFMYNEKA RVALENFFNR PDTLSVGVCN GCQLFVELGL
     INKDHAEKPK MLHNESHKHE SIFTSLTVAE NNSVMLSTLA GSTLGVWVSH GEGRFQLPYA
     EDKYRIVAKY AYESYPASPN GSDYNTAMLC DETGRHLVMM PHIERSLFQW HWANYPQGRK
     DEVSPWMEAF VNARKWIEGL RP
//
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