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Database: UniProt
Entry: M6F1J4_9LEPT
LinkDB: M6F1J4_9LEPT
Original site: M6F1J4_9LEPT 
ID   M6F1J4_9LEPT            Unreviewed;       330 AA.
AC   M6F1J4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=HpcH/HpaI aldolase/citrate lyase family protein {ECO:0000313|EMBL:EMK22638.1};
GN   ORFNames=LEP1GSC008_3506 {ECO:0000313|EMBL:EMK22638.1};
OS   Leptospira kirschneri serovar Bulgarica str. Nikolaevo.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1240687 {ECO:0000313|EMBL:EMK22638.1, ECO:0000313|Proteomes:UP000011980};
RN   [1] {ECO:0000313|EMBL:EMK22638.1, ECO:0000313|Proteomes:UP000011980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nikolaevo {ECO:0000313|EMBL:EMK22638.1,
RC   ECO:0000313|Proteomes:UP000011980};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA   Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:EMK22638.1}.
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DR   EMBL; ANCE01000163; EMK22638.1; -; Genomic_DNA.
DR   RefSeq; WP_004754013.1; NZ_ANCE01000163.1.
DR   AlphaFoldDB; M6F1J4; -.
DR   GeneID; 34316559; -.
DR   PATRIC; fig|1240687.3.peg.3351; -.
DR   OrthoDB; 8481499at2; -.
DR   Proteomes; UP000011980; 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; 6.10.140.960; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR040186; Citramalyl-CoA_lyase.
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; PTHR11105:SF0; CITRAMALYL-COA LYASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11105; CITRATE LYASE SUBUNIT BETA-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:EMK22638.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          51..243
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   330 AA;  37078 MW;  A1598DD6C8F26BCE CRC64;
     MSKLTHPREA LFEGEKPFPI IPACEHFAGS EKLITKALEL QNKLGGLFDI TMDCEDGAQT
     GKEKEHAELI VRLQNSELNK HKMSGVRIHD YTNSFWKQDV DIIVPGAGEK IAYITIPKPT
     RAAQVEEMIT YIQKAVQKAG IKREIPIHVL IETNGALQEV EKIAALPWLQ VLDFGLMDFI
     SGHHGAIPAS CMKSPGQFEH ELLRRGKANL VAAALANGVI PAHNVTLDLK NQYQTYKDAK
     RAHDDFGFLR MWSIYPTQIQ AILDAMAPDY SEVQTSAEIL IQAQNAEWGP IQYAGDLHDR
     ATYRYFWEIL QKAKLTGISI PEEANKRFFS
//
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