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Database: UniProt
Entry: A0A1R4G8H1_9MICO
LinkDB: A0A1R4G8H1_9MICO
Original site: A0A1R4G8H1_9MICO 
ID   A0A1R4G8H1_9MICO        Unreviewed;       269 AA.
AC   A0A1R4G8H1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Citrate lyase beta chain {ECO:0000313|EMBL:SJM64456.1};
DE            EC=4.1.3.6 {ECO:0000313|EMBL:SJM64456.1};
GN   ORFNames=CZ674_09825 {ECO:0000313|EMBL:SJM64456.1};
OS   Agrococcus casei LMG 22410.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=1255656 {ECO:0000313|EMBL:SJM64456.1, ECO:0000313|Proteomes:UP000195787};
RN   [1] {ECO:0000313|EMBL:SJM64456.1, ECO:0000313|Proteomes:UP000195787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22410 {ECO:0000313|EMBL:SJM64456.1,
RC   ECO:0000313|Proteomes:UP000195787};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUHU01000041; SJM64456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4G8H1; -.
DR   Proteomes; UP000195787; Unassembled WGS sequence.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
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:SJM64456.1};
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:UP000195787}.
FT   DOMAIN          2..198
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         109
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         109
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"
SQ   SEQUENCE   269 AA;  29210 MW;  44DB9128885AFB7A CRC64;
     MLVPASQPEL FDIAQQSRAD AVIIDVEDAV AANEKQQARK DTVEWLNSGH RAWVRINDAS
     SDFWSEDCAA LSKAEGLEGV MLAKSEGRSH LSDTADRLPQ GTRILALVET ARGIEHVEEI
     AHSNETFRIA FGTGDFRRDT ATGDSELALA YARSRMVIAS RAARLPAPID GPTLNRDKLL
     QGTQHARDMG MGGKLCLNHE HTGIINDSLA PSHEDIGWAH GFIKAFEASG GAITDGSDLP
     RLARAQRVVQ QAADFRIHVD AAEVGHNDY
//
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