ID A0A1C5H9I9_9ACTN Unreviewed; 318 AA.
AC A0A1C5H9I9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SCG42695.1};
GN ORFNames=GA0074704_1307 {ECO:0000313|EMBL:SCG42695.1};
OS Micromonospora siamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=299152 {ECO:0000313|EMBL:SCG42695.1, ECO:0000313|Proteomes:UP000198210};
RN [1] {ECO:0000313|EMBL:SCG42695.1, ECO:0000313|Proteomes:UP000198210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45097 {ECO:0000313|EMBL:SCG42695.1,
RC ECO:0000313|Proteomes:UP000198210};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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};
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DR EMBL; LT607751; SCG42695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5H9I9; -.
DR Proteomes; UP000198210; Chromosome i.
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:SCG42695.1};
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:UP000198210}.
FT DOMAIN 9..239
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 318 AA; 34235 MW; 68D1F09F74A90D4F CRC64;
MAAVGRPRRS CLAVPGSSVK MLGKAQGLPA DQVFLDLEDA VAPLAKPDAR KNIVAALNEG
DWAGKTRVVR VNDLTTSWTY RDVIEVVEGA GANLDCIMLP KVQNAGQVQW LDLTLTQIEK
TLGLPVGRIG IEAQIENAAG LVNVDAIAAA SPRVETIIFG PADFMASINM KSLVVGALIP
DYPGDPYHYI LMRILMAARM HDKQAIDGPF LQIRDVDAFR EVAKRSAALG FDGKWVLHPG
QIDAANEVYA PAQADYDHAE LILDAYEHYT SEAGGRLGAV MLGDEMIDEA SRKMALVISA
KGRAAGMTRT STFTPPER
//