ID B0S337_FINM2 Unreviewed; 1630 AA.
AC B0S337;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
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|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 OrderedLocusNames=FMG_1359 {ECO:0000313|EMBL:BAG08777.1};
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG08777.1, ECO:0000313|Proteomes:UP000001319};
RN [1] {ECO:0000313|EMBL:BAG08777.1, ECO:0000313|Proteomes:UP000001319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC {ECO:0000313|Proteomes:UP000001319};
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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|HAMAP-
CC Rule:MF_00138}.
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DR EMBL; AP008971; BAG08777.1; -; Genomic_DNA.
DR RefSeq; WP_012291021.1; NC_010376.1.
DR STRING; 334413.FMG_1359; -.
DR KEGG; fma:FMG_1359; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_003100_2_1_9; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000001319; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.40.50.880; -; 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 Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00138; GARS; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010141; FGAM_synthase.
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; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR01857; FGAM-synthase; 1.
DR NCBIfam; TIGR00877; purD; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01209; GARS_A; 1.
DR SMART; SM01210; GARS_C; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00138};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000001319}.
FT DOMAIN 107..309
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 866..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1480
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1601
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1630 AA; 183325 MW; 0637A87525436F8E CRC64;
MKILVVGSGG REFALGRKIK SFDESRKIFF APGNAGTESI GENVDIQADD LNGLLEFAKI
NNIDYTVVGP ENPLCDGISD LFEQNGLKIF GPVKEAAEFE NSKSFTKKFL GKYDIKTAKY
LESKDFDESY DFANKLLEEN GKVVVKRDGL AAGKGVYIVD NSDDLEKILK DVLEKDNMVV
IEQFLDGFEM SLLCFTDSKT ILPLPTAKDH KKIFERETGA NTGGMGTYAP NVEAEVFVDK
IKNSVLDKIL TGLKEENIDF RGLLFIGFMI TDDGIYVLEF NARFGDPETQ VVLELIDNDL
LDIMMKTSEG KLSDVDLKIN DNKALCIVLS AGGYPESYDK NDEITISDMD SYVFHAGTKK
VDGKIVTNGG RVLNIVNSKK NFDGVIKACY EDIEKVDFKN MYHRTDIGPR VKRVYVRKKD
EYDYESKEKK KQIENLLGID LDKFVIYKRY DLEISDDNLK KIVDTVLSEK SVDDVFYGED
ALKLQADMKN AIAVEYLPGQ FDQRKQGVLD TISLILDEDV DCKTSTVYEI EGASKQDLAK
IEKYLVNPVD SHKVNLLGIP TTLKQENPKN LENETYTNFR NMKDDELQKF VDDHSLAMND
EDLKCIRDYF KSEDRDPNET EIKILDTYWS DHCRHTTFNT FLDIEFNAKT KLDEAIHNSF
EEYLKVREEL KIEKPINLMS FGTILSKYMR SKNEFDDLEI SSEINACSVK IKVRVEVNGV
DETRDYLLMF KNETHNHPTE IEPFGGASTC LGGAIRDPLS GRAFVYQAMR ITGAGNPLTS
LEDTMDGKLP QIKITQEAAK GYSSYGNQIG LATGFVDEIY HDGYVAKRLE CGAVMAAAPI
ENVKRIEPEK GDIVILLGGR TGRDGIGGAT GSSKSHKVTS IKTESAQVQK GNAPEERKIQ
RLFRIPELAS LIKKCNDFGA GGVSVAIGEL HDGVDIYLDR VPLKYKGLKP FEIAISESQE
RMACVIAKKD LEEFVKYADA ENIETTVVAD ITDTNRMRMF YDEDLIADIS YDFINTNGSD
RNAEVEVVSE DVPEILTEKC SDANKFYEKV KQLNITSKRD LIEMFDSTIG RNTVINPMGG
KLQLNPSQAM VAKIPTMDGI MKTVSMMSYG FDADLSVQSQ YLGGYYAVVE SISKLIALGS
DKNLIRLTFQ EYYEKMLDKK IWSKPLKALL GAFTVSKYFK AMPIGGKDSM SGNFEDITVP
PTMISFAVTH EDVDNIITND LKGKGKIGLV RTPYEEDGTL NLEKLEENFD FITEQIRNKN
IISAIALDKK GLLANIFEQS VGNTGFNIKF DNLYNPMYGS FVVEYIDDDE NIEHIGEFSD
EIIVNDVKLD SEKLLEGYTQ VLNKVFTPKE KIEYKPIENK KIEQRRMKSK KPTDTPHVVI
LAAPGTNCEW DTLNAFKENG ADGEIVLFKN RNQEDILNSI DVLAEKIRKA QIFAIPGGFS
LGDEPDGSAK FLANILRNEK ISSAIDYLLN ENDGLVIGIC NGFQALVKTG LLPYGKVTSP
QEDDPNLTFN TNRRHIATFV DTLCLTNNSP WTNGIDLNKT YRMPISHGEG RFVIKEDKLQ
ELLDNEQVFS AYKISPNGSD YNIEGILSRD GKILGRMCHT ERIADDLYKN IYDIDKQNIF
RNAVEYFKEK
//
