ID A0A164TB90_9NOCA Unreviewed; 306 AA.
AC A0A164TB90;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:KZF13193.1};
GN ORFNames=A2J03_15220 {ECO:0000313|EMBL:KZF13193.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF13193.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF13193.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF13193.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-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:KZF13193.1}.
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DR EMBL; LVCV01000018; KZF13193.1; -; Genomic_DNA.
DR RefSeq; WP_068368308.1; NZ_LVCV01000018.1.
DR AlphaFoldDB; A0A164TB90; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000077673; 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:KZF13193.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000077673}.
FT DOMAIN 14..240
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 306 AA; 32674 MW; 87A62AC88A4BEBAE CRC64;
MTNQRPVRPR RSELSTPATS EKMMAKAAAG NADLVFLDLE DAVAPNAKDV ARKQAVTALR
ELDWGRKTRA VRINGVQTIW CLDDITEVVA GAGAHLDVLI IPKVKSARDV WFIDTLLTLL
EHKHGLEIGR IGLEVLIEEV EALAAVDAIA ASSPRLEALI LGVGDLAASH GMRSAHIGTS
SGYPGDIWHS ARTKMIVAAR SNGLDAIDGP FGDFKNDEAY LQQANWAAEL GAVGKWAIHP
SQVTLANEAY SPTEEAVAHA RKVVDAMRAA EATGDGAVAI DGIMVDAATA RIFETVLQRA
SVVEQH
//
