ID D6CL73_THIA3 Unreviewed; 427 AA.
AC D6CL73;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 68.
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 ECO:0000313|EMBL:CAZ87826.1};
GN OrderedLocusNames=THI_1132 {ECO:0000313|EMBL:CAZ87826.1};
OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ87826.1, ECO:0000313|Proteomes:UP000002372};
RN [1] {ECO:0000313|Proteomes:UP000002372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22701 / CIP 110005 / 3As
RC {ECO:0000313|Proteomes:UP000002372};
RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT "Structure, function, and evolution of the Thiomonas spp. genome.";
RL PLoS Genet. 6:E1000859-E1000859(2010).
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; FP475956; CAZ87826.1; -; Genomic_DNA.
DR RefSeq; WP_013105172.1; NZ_CTRL01000016.1.
DR AlphaFoldDB; D6CL73; -.
DR KEGG; thi:THI_1132; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_027420_3_1_4; -.
DR OrthoDB; 9807240at2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000002372; Chromosome.
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:UP000002372}.
FT DOMAIN 107..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 427 AA; 45609 MW; 348840BFD6CBE762 CRC64;
MKLLVIGSGG REHAIAWKLA QAPRVQKVYV SPGNGGTALD SRLENLQVAN AEELAAFCVR
EKIAYTVVGP EAPLAAGIVD GFRARGLKIF GPTRAAAQLE SSKAFSKDFM ARHHIPTAAY
ATFEDAAAAH AYVDKHGAPI VVKADGLAAG KGVVVAQTAD EAHAAIDDML QANRYGVQHN
AGRARVVIEE FLQGEEASFI VMVDGLHVLA LASSQDHKRL LDGDNGPNTG GMGAYSPAPV
VTPEVHARVM REIILPTVKG MAADGIPFTG FLYAGLMIDA QGRAKTLEFN CRMGDPETQP
IMARLKSDLS VVFEKAIAGQ LDQVELEWDR RTSLGVVLAA HGYPENPRKG DAITGIPPET
ADCITFHAGT TLDAQGVLRT SGGRVLVVTA LGDSPRIAQQ RAYEAIHTIH FDGMQCRRDI
GWRAIKR
//
