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Database: UniProt
Entry: M2YF21_9MICC
LinkDB: M2YF21_9MICC
Original site: M2YF21_9MICC 
ID   M2YF21_9MICC            Unreviewed;       303 AA.
AC   M2YF21;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Citrate lyase beta chain {ECO:0000313|EMBL:EME37140.1};
GN   ORFNames=C884_02054 {ECO:0000313|EMBL:EME37140.1};
OS   Kocuria palustris PEL.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME37140.1, ECO:0000313|Proteomes:UP000009877};
RN   [1] {ECO:0000313|EMBL:EME37140.1, ECO:0000313|Proteomes:UP000009877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEL {ECO:0000313|EMBL:EME37140.1,
RC   ECO:0000313|Proteomes:UP000009877};
RX   PubMed=24504000;
RA   Sharma G., Khatri I., Subramanian S.;
RT   "Draft Genome Sequence of Kocuria palustris PEL.";
RL   Genome Announc. 2:e01261-13(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EME37140.1}.
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DR   EMBL; ANHZ02000005; EME37140.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2YF21; -.
DR   STRING; 71999.KPaMU14_11890; -.
DR   Proteomes; UP000009877; 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; 2.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EME37140.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009877}.
FT   DOMAIN          11..93
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   DOMAIN          125..250
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   303 AA;  30933 MW;  D90C8B51F0A7837D CRC64;
     MTSSAQLATA RTALFSPALR PDRVLKAQGS GADCVVVDLE DAVAAADKDA AREHLIALLT
     GTHEAGALAG PVAVRINGPQ TEAGRADLEA LRRAARAHEH SASARAAAAA VGGSAPGCTE
     APELLDAVLI PKLESPEQVR DVRDGLGFEV GIVGTVESAA GLLALEEIVA DPGVVRLAVG
     ALDLAFDLGC GADSRTMAAA MARVVTVSRA RGLAGPLDSP TPEFRDLEPV RRAALRARED
     GFTGKLCIHP AQVEAAAEAF APTEEEIAWA RSVVEAVDGA SAVDGAMVDA PVIARARRLL
     GEG
//
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