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Database: UniProt
Entry: A0A060QFS2_9PROT
LinkDB: A0A060QFS2_9PROT
Original site: A0A060QFS2_9PROT 
ID   A0A060QFS2_9PROT        Unreviewed;       418 AA.
AC   A0A060QFS2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=ASAP_1949 {ECO:0000313|EMBL:CDG39994.1};
OS   Asaia bogorensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Asaia.
OX   NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG39994.1, ECO:0000313|Proteomes:UP000027583};
RN   [1] {ECO:0000313|EMBL:CDG39994.1, ECO:0000313|Proteomes:UP000027583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39994.1,
RC   ECO:0000313|Proteomes:UP000027583};
RX   PubMed=24682158; DOI=10.1093/gbe/evu062;
RA   Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA   Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT   "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT   life in insect guts.";
RL   Genome Biol. Evol. 6:912-920(2014).
RN   [2] {ECO:0000313|EMBL:CDG39994.1, ECO:0000313|Proteomes:UP000027583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39994.1,
RC   ECO:0000313|Proteomes:UP000027583};
RX   PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA   Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA   Lievens P.M., Daffonchio D., Bandi C.;
RT   "Evolution of mitochondria reconstructed from the energy metabolism of
RT   living bacteria.";
RL   PLoS ONE 9:e96566-e96566(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDG39994.1}.
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DR   EMBL; CBLX010000013; CDG39994.1; -; Genomic_DNA.
DR   RefSeq; WP_023978682.1; NZ_CBLX010000013.1.
DR   AlphaFoldDB; A0A060QFS2; -.
DR   eggNOG; COG0151; Bacteria.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000027583; 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; IPR020559; PRibGlycinamide_synth_CS.
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.
DR   PROSITE; PS00184; GARS; 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}.
FT   DOMAIN          107..313
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          216..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  43436 MW;  1A06528259EEDA35 CRC64;
     MRVLLVGSGG REHALAACLS RSPELETLFI APGNPGMQTL GTLVPLAADD VTALVNFARE
     QRIDLVVPGP EAPLVAGLAD LCAEAGIACA GPSQAASALE GSKSFTKDVA DAAGIPTARW
     ERFQEAEPAL AFVRRRGAPI VIKADGLAAG KGVIVALTLE EAEAAIIDIL TDRSFGAAGA
     SIVIEECLVG QEVSLFAFCS DGEAVLIGAA RDHKRIGEGD TGPNTGGMGA VSPPPNFDRD
     AQEKALDIMV RPMLAEMVRR GTPFRGIIFA GLMLTEDGPK LIEYNVRFGD PEAQALLIRL
     QSDLLPVLKA LAEGRLDDAA ISFTDEASIS VVLAARGYPG TPSKGGVIRG IERADAVPGV
     QVFQAGTAMQ DGKLVASGGR VLTVCATGAT PEEARARAYQ GVSAIDWDDG IYRRDIGL
//
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