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Database: UniProt
Entry: A0A1A2NBU9_9MYCO
LinkDB: A0A1A2NBU9_9MYCO
Original site: A0A1A2NBU9_9MYCO 
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
//
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