ID A0A1A2ZF25_9MYCO Unreviewed; 302 AA.
AC A0A1A2ZF25;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:OBI48102.1};
GN ORFNames=A5707_18505 {ECO:0000313|EMBL:OBI48102.1};
OS Mycobacterium kyorinense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=487514 {ECO:0000313|EMBL:OBI48102.1, ECO:0000313|Proteomes:UP000093592};
RN [1] {ECO:0000313|Proteomes:UP000093592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E861 {ECO:0000313|Proteomes:UP000093592};
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:OBI48102.1}.
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DR EMBL; LZKJ01000080; OBI48102.1; -; Genomic_DNA.
DR RefSeq; WP_065014040.1; NZ_LZKJ01000080.1.
DR AlphaFoldDB; A0A1A2ZF25; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000093592; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:OBI48102.1};
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 7..234
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 302 AA; 32632 MW; 65491C816D73FB71 CRC64;
MLLRRSELAV PASNDHMFAH AAGSGADLVF LDLEDAVAPA HKETARAKAI AALKELNWGR
TVRAIRINGL DTPWCHDDII DVVTQARDHL DTIIIPKVCT ARDVWWVDVL LTQLEAKLGL
GRPIALEVLI EEVEGLANAE QIAAASPRLD ALIFGVGDFS LSQGARVDTN FVPLGDYPGD
FWHYARNKVL VAARIAGIEA IDAPYPDYHD LEGYERDARR AGLLGYTGKW AIHPSQVPVA
NQVYAPTRAE IELAERNVAA YRDGEEKGLG AVGVDGVLVD AAHVKMAQAT LARAALIDGR
AG
//
