ID A0A0R1WQL6_9LACO Unreviewed; 379 AA.
AC A0A0R1WQL6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Phosphoribosylaminoimidazole carboxylase ncair mutase subunit {ECO:0000313|EMBL:KRM19733.1};
GN ORFNames=FC40_GL001337 {ECO:0000313|EMBL:KRM19733.1};
OS Ligilactobacillus hayakitensis DSM 18933 = JCM 14209.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423755 {ECO:0000313|EMBL:KRM19733.1, ECO:0000313|Proteomes:UP000051054};
RN [1] {ECO:0000313|EMBL:KRM19733.1, ECO:0000313|Proteomes:UP000051054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18933 {ECO:0000313|EMBL:KRM19733.1,
RC ECO:0000313|Proteomes:UP000051054};
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:KRM19733.1}.
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DR EMBL; AZGD01000033; KRM19733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1WQL6; -.
DR STRING; 1423755.FC40_GL001337; -.
DR PATRIC; fig|1423755.3.peg.1422; -.
DR eggNOG; COG0026; Bacteria.
DR Proteomes; UP000051054; 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:UP000051054}.
FT DOMAIN 115..301
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 379 AA; 42330 MW; ED09FE7BC518ED7F CRC64;
MTKMEHNALF PGNSIGIIGD GPNGIGIAQA AKKLGLKVIV YATNEGSPTL NEADVKMVGT
YNDKTKLQDF AERCDVVTYE SENISSDLIR YLSRFTNIPQ GFDTLEIVQD RLLERAMLED
LNVNIAPYAT IVSLDDIYQA VGSIGYPCVL KPIQKVFGNN KKQIIKKQTD IAKCAEFIDQ
GTYILESWIP HEKELSVSIT RNVDGVVNFF PIVETVYRDG KLEKSIVPAG LAKEVIDEVR
SIVSNIVTNL SYVGLLEVSF YLNKSGSLYV KSVVPTIHQA GYVFEKAANV SVFEQHIRTI
IDMPVGRVKL LQPIGMVMID EPRIEAVMTQ WVLKDNWTYT FFRYPESMNP KVEGYILVQG
DSAEAIKQQI ASTGIWDKE
//
