ID   V7JQ07_MYCAV            Unreviewed;       306 AA.
AC   V7JQ07;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Aldolase {ECO:0000313|EMBL:ETB00421.1};
GN   ORFNames=O982_03905 {ECO:0000313|EMBL:ETB00421.1};
OS   Mycobacterium avium 10-5581.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1392000 {ECO:0000313|EMBL:ETB00421.1, ECO:0000313|Proteomes:UP000018557};
RN   [1] {ECO:0000313|EMBL:ETB00421.1, ECO:0000313|Proteomes:UP000018557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-5581 {ECO:0000313|EMBL:ETB00421.1,
RC   ECO:0000313|Proteomes:UP000018557};
RA   Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT   "Genome sequence of MAC strains.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:ETB00421.1}.
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DR   EMBL; AYNT01000047; ETB00421.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7JQ07; -.
DR   PATRIC; fig|1392000.4.peg.838; -.
DR   Proteomes; UP000018557; 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}.
FT   DOMAIN          25..226
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   306 AA;  33222 MW;  E883D996CDDAC74C CRC64;
     MYEQVNSSAA EPDDIGSRID PVLARSWLLV NGTHPDRFQS AVNSRADIVV FDIEDAVAPK
     DKNAARDNVV SWLRAGNVDW VRINGFGTPW WADDLTALAG TPVGGVMLAM VESVDHVTET
     AKRLPDVPIV ALVETARGLE RITEIAATKG TFRLAFGIGD FRRDTGFGED PATLAYTRSR
     FTIASKAADL PSAIDGPTIG SNPLKLIEAT AVSTQFGMTG KICLTPDQCS VVNEGLSPSQ
     DEIAWAKEFF AEFERDGGEI RNGSDLPRIA RATKILELAR AYGIEALDID EEERDHSPAP
     SDTYHY
//