ID A0A0R1RQQ5_9LACO Unreviewed; 372 AA.
AC A0A0R1RQQ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ATP-grasp domain protein {ECO:0000313|EMBL:KRL59057.1};
GN ORFNames=FC69_GL001921 {ECO:0000313|EMBL:KRL59057.1};
OS Latilactobacillus fuchuensis DSM 14340 = JCM 11249.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=1423747 {ECO:0000313|EMBL:KRL59057.1, ECO:0000313|Proteomes:UP000051264};
RN [1] {ECO:0000313|EMBL:KRL59057.1, ECO:0000313|Proteomes:UP000051264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14340 {ECO:0000313|EMBL:KRL59057.1,
RC ECO:0000313|Proteomes:UP000051264};
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).
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:KRL59057.1}.
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DR EMBL; AZEX01000056; KRL59057.1; -; Genomic_DNA.
DR RefSeq; WP_025083247.1; NZ_BAMJ01000015.1.
DR AlphaFoldDB; A0A0R1RQQ5; -.
DR STRING; 1423747.FC69_GL001921; -.
DR PATRIC; fig|1423747.3.peg.1951; -.
DR eggNOG; COG0026; Bacteria.
DR OrthoDB; 9804625at2; -.
DR Proteomes; UP000051264; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; 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}.
FT DOMAIN 112..298
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 372 AA; 41687 MW; F8DFAD642D4203B5 CRC64;
MPVIYPGQMI GIIGNDQRAF LLALAAKKMG YKVAMIVNAQ IQDTPLASIL DAQVEGDPNQ
YADLARLGDI CQVLTYTDEL LDETLLEQLA QNYYLPQGSS VLSVTQDRYL ERVFLDDLNI
NIPPSTTVVD VEDIQQGIDS IGYPCILKPI QKGFGKQYQR FIKEPADLDQ LTDFLQLGSY
LLESWIPDAQ ELSVMVAKDV QGDLTVLPIV ENDYQDHQLR LSIVPARIDQ TVAAEINRLA
NLIGQKLDYV GVFGIEFFLT PDMNIYVKRL VPTPHISGNV LERTLNFSQY EYHLKAICQL
ALGEARLNNA GVTLNIQEAS LPLVKTQMKI KPDWYFNLYH LQDRQQFGSL TAIGAAVNPL
LEKLEAADLY HA
//