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Database: UniProt
Entry: A0A1G1TIW7_9BACT
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ID   A0A1G1TIW7_9BACT        Unreviewed;       426 AA.
AC   A0A1G1TIW7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-MAY-2019, entry version 12.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138};
GN   ORFNames=BEN49_00490 {ECO:0000313|EMBL:OGX90807.1};
OS   Hymenobacter coccineus.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1908235 {ECO:0000313|EMBL:OGX90807.1, ECO:0000313|Proteomes:UP000177506};
RN   [1] {ECO:0000313|EMBL:OGX90807.1, ECO:0000313|Proteomes:UP000177506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8649 {ECO:0000313|EMBL:OGX90807.1,
RC   ECO:0000313|Proteomes:UP000177506};
RA   Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E.,
RA   Vrbovska V., Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT   "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT   Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, 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;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OGX90807.1}.
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DR   EMBL; MDZA01000111; OGX90807.1; -; Genomic_DNA.
DR   RefSeq; WP_070742611.1; NZ_MDZA01000111.1.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000177506; 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; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.600.10; -; 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; IPR020559; PRibGlycinamide_synth_CS.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00877; purD; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000177506};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:OGX90807.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      104    309       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   426 AA;  44837 MW;  12108A4EF6226A78 CRC64;
     MKPIILLGSG AREHAMAAKL TRDGASVQVV PGNAGIPNSH PGLDPLDFAA LEAYARHQGV
     QLIVVGPEAP LAAGVADYFA GSDIEVFGPT KAGALLESSK VWSKDFMRRY GVATAQAWPF
     RSDEIAAARA KAAELGGQVV VKYDGLAAGK GVYVCGSLAE AEAALDDLQA HYTGWYSFLL
     EERLTGPEIS IIGLTDGHEM KLLATSQDHK QLLAGDEGPN TGGMGAYCPV PFADDNVLAD
     IRRDIVEPTL RGLQNEQFEF RGFLYFGIML TPTGPKLLEY NVRLGDPEAE VLLPAMDSSL
     LTLIEATLDG SLAQQAVRQR PGAYVGVVLA SGGYPASGFP TGFPITGLEN LPVGVEAFHG
     ATKRNAEGQL VTNGGRVLVL SAQGPTLAAA TALAYEAAGL VAFQDKYVRP DIAQRPAPVL
     TQRAVN
//
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