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Database: UniProt
Entry: A0A166UI11_9CYAN
LinkDB: A0A166UI11_9CYAN
Original site: A0A166UI11_9CYAN 
ID   A0A166UI11_9CYAN        Unreviewed;       427 AA.
AC   A0A166UI11;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUN-2019, entry version 16.
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=AY599_02455 {ECO:0000313|EMBL:OAB61732.1};
OS   Leptolyngbya valderiana BDU 20041.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=322866 {ECO:0000313|EMBL:OAB61732.1};
RN   [1] {ECO:0000313|EMBL:OAB61732.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDU 20041 {ECO:0000313|EMBL:OAB61732.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAB61732.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDU 20041 {ECO:0000313|EMBL:OAB61732.1};
RA   Peter A.P., Garlapati D., Kaliaperumal E.M., Lakshmanan K.,
RA   Tyagaraj B.;
RT   "De novo Whole Genome Sequencing of Leptolyngbya valderiana BDU
RT   20041.";
RL   Submitted (MAY-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:OAB61732.1}.
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DR   EMBL; LSYZ01000112; OAB61732.1; -; Genomic_DNA.
DR   RefSeq; WP_063716583.1; NZ_LSYZ01000112.1.
DR   EnsemblBacteria; OAB61732; OAB61732; AY599_02455.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; GCF_001637395:G1ET2-2453-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
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   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:OAB61732.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      109    315       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      211    235       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A166UI11}.
SQ   SEQUENCE   427 AA;  45431 MW;  CFDBD4F8679D3809 CRC64;
     MKVLVIGGGG REHALAWKVA QSERVDEVLV APGNAGTAGE AKCRNVPVAA EDIDALLALA
     QKEAVDLTIV GPEAPLAAGV VDRFTAAGLA CFGPDAGAAQ LESSKAFAKD FMARHEIPTA
     AYGVAETLEQ GLELIRSIGL PLVLKADGLA AGKGVVIVET ETEAEATLRD MLSGESFGEA
     GRRVVIEEFL EGEEASFIVI ADGLKALPLA TSQDHKRRDE GDRGPNTGGM GAYSPAPVVT
     PELHRQILDE IIRPTLAGMQ SDGHSFTGFL YAGVMLTERG PKVLEFNVRF GDPETQPVMM
     RLRSDLVEVL ERTLKGELDR IELDWDPRVA LGVVVAAGGY PEAYEKGKAI DGLDRELPED
     VRVFHAGTRL GEDGRILTSG GRVLCVTALG KDVGSARERA LEAASTIHFD QAFLRRDIGH
     RALSREA
//
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