ID A0A1A2NBU9_9MYCO Unreviewed; 307 AA.
AC A0A1A2NBU9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Aldolase {ECO:0000313|EMBL:OBH12561.1};
GN ORFNames=A5695_16160 {ECO:0000313|EMBL:OBH12561.1};
OS Mycobacterium sp. E1747.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834128 {ECO:0000313|EMBL:OBH12561.1, ECO:0000313|Proteomes:UP000092218};
RN [1] {ECO:0000313|Proteomes:UP000092218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1747 {ECO:0000313|Proteomes:UP000092218};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
RL Submitted (JUN-2016) 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:OBH12561.1}.
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DR EMBL; LZJI01000048; OBH12561.1; -; Genomic_DNA.
DR RefSeq; WP_068078767.1; NZ_LZJI01000048.1.
DR AlphaFoldDB; A0A1A2NBU9; -.
DR STRING; 1834128.A5695_16160; -.
DR OrthoDB; 4322898at2; -.
DR Proteomes; UP000092218; 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|PIRSR:PIRSR015582-2}.
FT DOMAIN 26..227
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 288..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 307 AA; 33204 MW; EC7CCC45A19F47C8 CRC64;
MYDQVNSSAT EPDDVIGYRI DPVLARSWLL VNGAHADRFQ SATHSRADIV VLDIEDAVAP
KDKHAARDNV VSWLAAGNTD WVRVNGFGTP WWADDLAALS GTPVGGVMLA MVESVDHVTE
TAQRLPNVPI VALVETARGL ERITEIAAAK GTFRLAFGIG DFRRDTGFGE HPSTLAYARS
RFTIAAKAAS LPSAIDGPTI GSNALKLIEA TAVSVEFGMT GKICLTPDQC GVVNEGLSPS
QDEIAWAKEF FAEFERDGGE IRNGSDLPRI ARATKILELA RAYDIESSDF DDEERDHSPA
PSDTYHY
//