ID A0A0R1JB01_9LACO Unreviewed; 376 AA.
AC A0A0R1JB01;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000313|EMBL:KRK65210.1};
GN ORFNames=FC72_GL001586 {ECO:0000313|EMBL:KRK65210.1};
OS Companilactobacillus tucceti DSM 20183.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1423811 {ECO:0000313|EMBL:KRK65210.1, ECO:0000313|Proteomes:UP000050929};
RN [1] {ECO:0000313|EMBL:KRK65210.1, ECO:0000313|Proteomes:UP000050929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20183 {ECO:0000313|EMBL:KRK65210.1,
RC ECO:0000313|Proteomes:UP000050929};
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:KRK65210.1}.
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DR EMBL; AZDG01000004; KRK65210.1; -; Genomic_DNA.
DR RefSeq; WP_057764622.1; NZ_AZDG01000004.1.
DR AlphaFoldDB; A0A0R1JB01; -.
DR STRING; 1423811.FC72_GL001586; -.
DR PATRIC; fig|1423811.3.peg.1612; -.
DR OrthoDB; 9804625at2; -.
DR Proteomes; UP000050929; 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:UP000050929}.
FT DOMAIN 110..296
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 376 AA; 42843 MW; 1CFF08479C50FC66 CRC64;
MTFIAPGKTL GIIGGGSETY LFELEAKRMG FRTVLLTTEE DDIATQAADT YLVGDLEDSD
NLTELGHRSD ILLYMDENFD SDILESLERE FNVVQGSNML AIVQDRYIER TFLNSLKINV
PPFFSIVTVD DIKKAVEEIG FPCMIKPIQK NQNVLRRHVL YNETDVEHVQ NLLANGTYIL
EAWIDTKEEY SIMVSKSKNG KIHTFPMIRE IYDGSHLMSS YLYKKNDPEV EAEIQRVALI
IANNIEYVGI FGIGFIISDS GVLYVKRIFP GINYSANVYQ EATGVSQFEL HIRAICDWPI
PEIYPLINAA TLKIIEGNLP QSLDLLQEKA QWKFNYYTGF KAKNDAARDV GYISVVSDEE
EDLREDILST KIWRVE
//
