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Database: UniProt
Entry: A0A0R2L6Y6_9LACO
LinkDB: A0A0R2L6Y6_9LACO
Original site: A0A0R2L6Y6_9LACO 
ID   A0A0R2L6Y6_9LACO        Unreviewed;       396 AA.
AC   A0A0R2L6Y6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Phosphoribosylaminoimidazole carboxylase, atpase subunit {ECO:0000313|EMBL:KRN95669.1};
DE   SubName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000313|EMBL:GEK28068.1};
GN   Name=purK2 {ECO:0000313|EMBL:GEK28068.1};
GN   ORFNames=IV55_GL001770 {ECO:0000313|EMBL:KRN95669.1}, LSI01_03790
GN   {ECO:0000313|EMBL:GEK28068.1};
OS   Furfurilactobacillus siliginis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Furfurilactobacillus.
OX   NCBI_TaxID=348151 {ECO:0000313|EMBL:KRN95669.1, ECO:0000313|Proteomes:UP000051139};
RN   [1] {ECO:0000313|EMBL:KRN95669.1, ECO:0000313|Proteomes:UP000051139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22696 {ECO:0000313|EMBL:KRN95669.1,
RC   ECO:0000313|Proteomes:UP000051139};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
RN   [2] {ECO:0000313|EMBL:GEK28068.1, ECO:0000313|Proteomes:UP000321429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101315 {ECO:0000313|EMBL:GEK28068.1,
RC   ECO:0000313|Proteomes:UP000321429};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Lactobacillus siliginis NBRC 101315.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025704}.
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:KRN95669.1}.
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DR   EMBL; BJUD01000003; GEK28068.1; -; Genomic_DNA.
DR   EMBL; JQCB01000007; KRN95669.1; -; Genomic_DNA.
DR   RefSeq; WP_057810351.1; NZ_JQCB01000007.1.
DR   AlphaFoldDB; A0A0R2L6Y6; -.
DR   STRING; 348151.IV55_GL001770; -.
DR   PATRIC; fig|348151.3.peg.1821; -.
DR   OrthoDB; 9804625at2; -.
DR   Proteomes; UP000051139; Unassembled WGS sequence.
DR   Proteomes; UP000321429; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR   PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051139};
KW   Transferase {ECO:0000313|EMBL:GEK28068.1}.
FT   DOMAIN          112..304
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   396 AA;  43627 MW;  9F53CE8D6432DCCD CRC64;
     MAGTILYPGN TLGIIGNSSN GPLLVNAARR VGLNVAAYTS EGDSEIASLA DAVFVGAFDD
     QQRLQAFAEN CDIVTYESEH VPSDVIAFIS RFTKVPQTSD ALAMMQDRSL ERAFFEELKI
     NIPPYATIIG LDDLYGSAAG IGYPAILKPM QKGIEHEQQL TIRSQADVPL AADMLQKGPH
     ILEATVPKAQ ELSVLVVKGY PQENELADQI RLFPIIETNY QQGRLMRALA PARISNDVAG
     EVDRISQTVA QHLDYYGVFQ LTFLLTPEGT LFLRDLVPAM DRSGLVFDKA TNITMFEAHL
     HAIAGLPLAK PQQYMTAVLA SFDDDQLDAI RTQWILKSNW EFVFYHRSGR QISPTAGHVL
     IQAPTIQDGL NQLAATTIWD PRRPLPPTPS RLNNRV
//
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