ID A0A0X1TK16_9FIRM Unreviewed; 417 AA.
AC A0A0X1TK16;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AT726_05500 {ECO:0000313|EMBL:AMC08428.1};
OS Turicibacter sp. H121.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Turicibacteraceae; Turicibacter.
OX NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC08428.1, ECO:0000313|Proteomes:UP000057144};
RN [1] {ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC08428.1, ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|EMBL:AMC08428.1,
RC ECO:0000313|Proteomes:UP000057144};
RX PubMed=27013036;
RA Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT the Feces of a Contaminated Germ-Free Mouse.";
RL Genome Announc. 4:0-0(2016).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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; CP013476; AMC08428.1; -; Genomic_DNA.
DR RefSeq; WP_068759202.1; NZ_JAMQUX010000001.1.
DR AlphaFoldDB; A0A0X1TK16; -.
DR STRING; 1712675.AT726_05500; -.
DR KEGG; tur:AT726_05500; -.
DR OrthoDB; 9807240at2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000057144; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000057144}.
FT DOMAIN 106..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 417 AA; 45618 MW; DD55C1CE0F222A1D CRC64;
MKVLVIGRGG REHAVVKKLA CDSKVTEIFC APGNDGMIEA TLVPIEETDV NALANFAKKN
QIDLTIVGPE MTLMAGVVNK FKELDLPVFG PTKEAALIEG SKSFAKYMMS KYNIPTAAYG
EFTQVEEALA YLETQSMPIV IKADGLAAGK GVVICQTLEE ANQTVKEMLL DRKFEDASSK
VVIEEFLDGE EFSLMAFVSN DIYKAMPIAR DYKRAYDNDK GLNTGGMGNH SPHPLILDTD
YEEAIQTVIE PMTKAMIEEG IPFTGILYAG LMKTANGIKV IEFNARFGDP ETEVLLPRLE
TELTDIIFSL LDGKDIECVW SDQATVGVVL AAKGYPSSYV KGTVIEGLEN LVDVDVCHMG
TKLVDGKITL NGGRVLFVVG SGNTLEEARQ KVYKEIQKIN CDDLFYRTDI AKKATSC
//
