ID F0NZ19_WEEVC Unreviewed; 420 AA.
AC F0NZ19;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=Weevi_1536 {ECO:0000313|EMBL:ADX68236.1};
OS Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / CCUG 30538 /
OS CDC 9751 / IAM 14551 / NBRC 16016 / NCTC 11634 / CL345/78).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Weeksella.
OX NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX68236.1, ECO:0000313|Proteomes:UP000008641};
RN [1] {ECO:0000313|EMBL:ADX68236.1, ECO:0000313|Proteomes:UP000008641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX PubMed=21475590;
RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Kopitz M., Rohde M., Goker M., Tindall B.J., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Weeksella virosa type strain (9751).";
RL Stand. Genomic Sci. 4:81-90(2011).
RN [2] {ECO:0000313|Proteomes:UP000008641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX DOI=10.4056/sigs.1603927;
RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Brambilla E.,
RA Kopitz M., Rohde M., Goker M., Tindall B., Detter J., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.;
RT "Complete genome sequence of Weeksella virosa type strain (9751T).";
RL Stand. Genomic Sci. 4:81-90(2011).
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; CP002455; ADX68236.1; -; Genomic_DNA.
DR RefSeq; WP_013598625.1; NC_015144.1.
DR AlphaFoldDB; F0NZ19; -.
DR STRING; 865938.Weevi_1536; -.
DR KEGG; wvi:Weevi_1536; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_027420_3_1_10; -.
DR OrthoDB; 9807240at2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000008641; 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:UP000008641}.
FT DOMAIN 111..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 420 AA; 46314 MW; E821D402851A00B0 CRC64;
MSTKILIVGS GGREHAIGWK FAEDFKRKQE KVDLFFVPGN AGTAKLGENI ALNSITEMKD
FALENKIDLT FVGPEAELAE GIVDLFQANH LPIFGPHREA AKLESSKAFA KDFMHKYGVK
TAEYKVFQGP MLAIEYLEKA SFPIVIKASG LAAGKGVIIC QDFDQAKKAV LEIMEDKTFG
DAGNEVVIEE YLEGFEASIL SFFNGKTIIP FISAKDHKKI GEGETGLNTG GMGAIAPNPL
FTEAHYQAFL EDVLEPTKCG LIKEGLRFSG VIFFGLMITT KGVYLLEYNL RMGDPETQTT
LPLLENDLYD VVQKTIKNEE FTLEFSAQHS CCVVMVSGGY PGNYEKGYPI RGLDQVTCPT
FIAGAKLSQQ EILTSGGRVL NVVGIGKSLE EARKTAYENV AKIHFDYEYY RNDIGEIKKK
//
