ID A0A0R1PHU4_9LACO Unreviewed; 396 AA.
AC A0A0R1PHU4;
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 {ECO:0000313|EMBL:KRL28120.1};
GN ORFNames=FD27_GL000394 {ECO:0000313|EMBL:KRL28120.1};
OS Limosilactobacillus frumenti DSM 13145.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423746 {ECO:0000313|EMBL:KRL28120.1, ECO:0000313|Proteomes:UP000051445};
RN [1] {ECO:0000313|EMBL:KRL28120.1, ECO:0000313|Proteomes:UP000051445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13145 {ECO:0000313|EMBL:KRL28120.1,
RC ECO:0000313|Proteomes:UP000051445};
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 -!- 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:KRL28120.1}.
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DR EMBL; AZER01000013; KRL28120.1; -; Genomic_DNA.
DR RefSeq; WP_057749349.1; NZ_AZER01000013.1.
DR AlphaFoldDB; A0A0R1PHU4; -.
DR STRING; 1423746.FD27_GL000394; -.
DR PATRIC; fig|1423746.3.peg.402; -.
DR OrthoDB; 9804625at2; -.
DR Proteomes; UP000051445; 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: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:UP000051445}.
FT DOMAIN 112..297
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 371..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 44130 MW; D3092A123E5BC998 CRC64;
MSTKPIFPGS TLGIIGINRN GGALISCAKK AGFNVGVYVD RAQPNITKMA DFTLDGAYND
KEKLMQFGEA CDAIIYQTPN IDSSVLRYLG QYAAIPQGIN GLEIVQDRLM ERAFLDQVNI
NIAPYVTVIG LDDVYQSIDS IGYPALLKPI QRGIGEQSMI IRRQSDITRA AEFIDTGTYL
LESWIEHTHE YTMTAAVSGD DLQIFPVAEL NYDDDRQLIS AAAPAEVNDD MATEMRRIVK
SVAASLQYTG VFSINFYVTS TGTLYVKNIE LGLTSIANVY DSTTNVNQYE EQIRAVVGMP
IHNITNLQSG LLMVVRNYQS RAIQRQWLLK DNWQFRFFND VDGNDPQALL GFVWVTGEED
LQALQEQVDN TEVWNTKPAE PTTDEQADQG QSETNE
//
