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Database: UniProt
Entry: I0RJL1_MYCXE
LinkDB: I0RJL1_MYCXE
Original site: I0RJL1_MYCXE 
ID   I0RJL1_MYCXE            Unreviewed;       305 AA.
AC   I0RJL1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN   ORFNames=MXEN_16797 {ECO:0000313|EMBL:EID11314.1};
OS   Mycobacterium xenopi RIVM700367.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID11314.1, ECO:0000313|Proteomes:UP000003584};
RN   [1] {ECO:0000313|EMBL:EID11314.1, ECO:0000313|Proteomes:UP000003584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIVM700367 {ECO:0000313|EMBL:EID11314.1,
RC   ECO:0000313|Proteomes:UP000003584};
RX   PubMed=22628510; DOI=10.1128/JB.00482-12;
RA   Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA   van Soolingen D., Bitter W., Pain A.;
RT   "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL   J. Bacteriol. 194:3282-3283(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EID11314.1}.
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DR   EMBL; AJFI01000083; EID11314.1; -; Genomic_DNA.
DR   RefSeq; WP_003922226.1; NZ_AJFI01000083.1.
DR   AlphaFoldDB; I0RJL1; -.
DR   PATRIC; fig|1150591.3.peg.3388; -.
DR   OrthoDB; 4322898at2; -.
DR   Proteomes; UP000003584; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003584}.
FT   DOMAIN          25..224
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   305 AA;  32837 MW;  4131AC5C22F972AA CRC64;
     MSEQIETTAP DATRVGSRID PVLARSWLLV NGAHPDRFDD AARSTADIVV LDIEDAVAPK
     DKAAARDNVV RWLGAGNSDW VRINGFGTPW WADDLAMLAG TSVGGVMLAM VESVDHVTET
     AKRVPNVPIV ALVETARGLE RITEIAAAKG TFRLAFGIGD FRRDTGFGED TATLAYARSR
     FTIAAKAANL PSAIDGPTIG SNPLKLIEAT AVSAEFGMTG KICLTPDQCP VVNEGLSPSQ
     DEIAWAKEFL AEFERDGGEI RNGSDLPRFA RATKILELAR AYGIKISHFD DEPVHMPAPS
     DTYHY
//
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