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Database: UniProt
Entry: A0A1X1YJP8_9MYCO
LinkDB: A0A1X1YJP8_9MYCO
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ID   A0A1X1YJP8_9MYCO        Unreviewed;       422 AA.
AC   A0A1X1YJP8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
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=AWC16_11775 {ECO:0000313|EMBL:ORW11241.1};
OS   Mycolicibacter longobardus.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=1108812 {ECO:0000313|EMBL:ORW11241.1, ECO:0000313|Proteomes:UP000193866};
RN   [1] {ECO:0000313|EMBL:ORW11241.1, ECO:0000313|Proteomes:UP000193866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45394 {ECO:0000313|EMBL:ORW11241.1,
RC   ECO:0000313|Proteomes:UP000193866};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S.,
RA   Sara T., Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R.,
RA   Monica P., Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-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:ORW11241.1}.
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DR   EMBL; LQPG01000018; ORW11241.1; -; Genomic_DNA.
DR   BioCyc; GCF_002102265:AWC16_RS10460-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000193866; 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:UP000193866};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:ORW11241.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      107    312       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   422 AA;  43187 MW;  3FA9BA71F3A7F3F6 CRC64;
     MRILVIGSGA REHALLMALR NDPKVDHLVI APGNAGTAAV AEQRDIDITS ASAVTDLARE
     VKADLVVIGP EVPLVLGVAD AVRAAGIACF GPSQDAARIE GSKAFAKDVM AAAGVRTARS
     EIVDSPADLD AALSRFGPEA GEAAWVVKDD GLAAGKGVVV TADRSAARAH AAGLLEAGHP
     VLLESFLDGP ELSLFCIVDG TTVVPLLPAQ DFKRVGDDDT GPNTGGMGAY APLPWLSRQA
     AAGIVASVVE PVAVELLRRG SRFTGLLYAG LAMTSTGPAV VEFNCRFGDP ETQAVLALLE
     SPLGQLLHAA ATGRLSEFGA LRWRDGAAVT VVLAAENYPG RPRVGDVIVG AEADGVLHAG
     TARRDDGAVV SSGGRVLSVV GTGEDLSAAR ADAYRILSSI RLPGSHFRTD IGLAAAEGKI
     EI
//
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