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Database: UniProt
Entry: A0A1C5H9I9_9ACTN
LinkDB: A0A1C5H9I9_9ACTN
Original site: A0A1C5H9I9_9ACTN 
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
//
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