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
//