ID   A0A0S7CSX7_9MICC        Unreviewed;       278 AA.
AC   A0A0S7CSX7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Citrate lyase subunit beta-like protein {ECO:0000313|EMBL:GAP58142.1};
GN   ORFNames=AHiyo1_11370 {ECO:0000313|EMBL:GAP58142.1};
OS   Arthrobacter sp. Hiyo1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1588020 {ECO:0000313|EMBL:GAP58142.1};
RN   [1] {ECO:0000313|EMBL:GAP58142.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hiyo1 {ECO:0000313|EMBL:GAP58142.1};
RX   PubMed=26764021; DOI=10.1186/s12864-016-2380-4;
RA   Hiraoka S., Machiyama A., Ijichi M., Inoue K., Oshima K., Hattori M.,
RA   Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Genomic and metagenomic analysis of microbes in a soil environment
RT   affected by the 2011 Great East Japan Earthquake tsunami.";
RL   BMC Genomics 17:53-53(2016).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; DF952469; GAP58142.1; -; Genomic_DNA.
DR   RefSeq; WP_059387830.1; NZ_DF952469.1.
DR   AlphaFoldDB; A0A0S7CSX7; -.
DR   OrthoDB; 5172636at2; -.
DR   Proteomes; UP000063628; 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:GAP58142.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          9..218
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   278 AA;  29038 MW;  4D5078B4750E45AE CRC64;
     MTFTMGPALL FCPADRSERF QKAAERSDAV IVDLEDAVAP ADKKRARGAI LAQLGSGGET
     AELDPSRTIV RVNPVGTPDF EKDLHCLAHT PYRTIMLAKA ETAEQLKALE GYHVIALCET
     AKGIVNAAEI AQAPNVVGLM WGAEDLIASM GGTSSRKDDG GYRAVATHSR STVLLAAKAA
     GKEAIDSVYV DIPDLAGLAV ESADAVASGF GAKACIHPNQ VAVVREAYAP SPEAVAVARE
     LLDAAAAAGT GVFQHKGKMV DGPILKHAES TLRRARLS
//