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Database: UniProt
Entry: A0A1I1NE75_9FLAO
LinkDB: A0A1I1NE75_9FLAO
Original site: A0A1I1NE75_9FLAO 
ID   A0A1I1NE75_9FLAO        Unreviewed;       423 AA.
AC   A0A1I1NE75;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242, ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864, ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138};
GN   ORFNames=SAMN04487987_102228 {ECO:0000313|EMBL:SFC95795.1};
OS   Algibacter pectinivorans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Algibacter.
OX   NCBI_TaxID=870482 {ECO:0000313|EMBL:SFC95795.1, ECO:0000313|Proteomes:UP000199439};
RN   [1] {ECO:0000313|Proteomes:UP000199439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25730 {ECO:0000313|Proteomes:UP000199439};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005174,
CC       ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|ARBA:ARBA00038345,
CC       ECO:0000256|HAMAP-Rule:MF_00138}.
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DR   EMBL; FOMI01000002; SFC95795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1NE75; -.
DR   STRING; 870482.SAMN04487987_102228; -.
DR   OrthoDB; 9807240at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000199439; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR00877; purD; 1.
DR   PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR   PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01209; GARS_A; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00138};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00138}; Reference proteome {ECO:0000313|Proteomes:UP000199439}.
FT   DOMAIN          111..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   423 AA;  46295 MW;  40D5BACF28E4B60D CRC64;
     MNILILGSGG REHTFAWKIA QSPKCDKLFV APGNSGTNEI ATNVNIGVTD FPAIKELVLS
     NHIDLVVVGP EDPLVQGVHD FFLNDDAIKH VSVIGPQKAA AELEGSKEFA KEFLYRHNIP
     TAAYESFTKE TVEKGYAFLE TLNAPYVLKA DGLAAGKGVV ILNDINEAKA ELKSMLVDAK
     FGEASTKVVI EEFLDGIELS CFVLTDGEHY KILPTAKDYK RIGEGDTGLN TGGMGAVSPV
     PFATDEFLNK IEERIVKPTI AGFKKDKLPY VGFVFIGLIK VGDDPKVIEY NVRMGDPETE
     VVLPRLKNDF VDILQAMAHG TLNNIDIEID ERAATTIMTV SGGYPEAYEK GKEITGVETI
     EDSIPFHAGA QIKDGKIVTS GGRVMAITSY GNTYQEAIKK SYQSIEKLHF DKMYYRKDIG
     FDL
//
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