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Database: UniProt
Entry: A0A0D1J3H7_9MYCO
LinkDB: A0A0D1J3H7_9MYCO
Original site: A0A0D1J3H7_9MYCO 
ID   A0A0D1J3H7_9MYCO        Unreviewed;       305 AA.
AC   A0A0D1J3H7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Aldolase {ECO:0000313|EMBL:KIU16158.1};
GN   ORFNames=TL10_14545 {ECO:0000313|EMBL:KIU16158.1};
OS   Mycolicibacterium llatzerense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU16158.1, ECO:0000313|Proteomes:UP000032221};
RN   [1] {ECO:0000313|EMBL:KIU16158.1, ECO:0000313|Proteomes:UP000032221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLUC14 {ECO:0000313|EMBL:KIU16158.1,
RC   ECO:0000313|Proteomes:UP000032221};
RA   Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT   recovered from brain abscess.";
RL   Submitted (JAN-2015) 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:KIU16158.1}.
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DR   EMBL; JXST01000019; KIU16158.1; -; Genomic_DNA.
DR   RefSeq; WP_043393772.1; NZ_LXSC01000017.1.
DR   AlphaFoldDB; A0A0D1J3H7; -.
DR   STRING; 280871.TL10_14545; -.
DR   PATRIC; fig|280871.6.peg.3023; -.
DR   OrthoDB; 4322898at2; -.
DR   Proteomes; UP000032221; 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:UP000032221}.
FT   DOMAIN          25..195
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;  33074 MW;  5EA9EE2F9C492A99 CRC64;
     MYDQPSTYEP DANEHGSRLD PVLARSWLLV NGAQFDRFSP ATRSPADIVI VDIEDAVAPK
     DKDSARDNAA RWLGEGNTDW VRVNGFGTPW WADDLEMLSK TSVGGIMLAM VESVDHVTET
     AKRLPNVPIV ALVETARGLE RITEIASAKG TFRLAFGIGD FRRDTGFGDN PATLAYARSR
     FTIAAKAAHL PGAIDGPTIG SSSRKLSEAT AVSIEFGMTG KICLTPEQCG TVNEGLSPSL
     DEIAWAQEFF AEFERDGGEI RNGSDLPRIA RANKILDLAK AYGIHPSMFG DDPDHVSAPS
     DTYHY
//
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