ID   A0A136KUG0_9CHLR        Unreviewed;       288 AA.
AC   A0A136KUG0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:KXK12963.1};
GN   Name=citE {ECO:0000313|EMBL:KXK12963.1};
GN   ORFNames=UZ14_CFX002002009 {ECO:0000313|EMBL:KXK12963.1};
OS   Chloroflexi bacterium OLB14.
OC   Bacteria; Chloroflexota; Tepidiformia.
OX   NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK12963.1, ECO:0000313|Proteomes:UP000070321};
RN   [1] {ECO:0000313|EMBL:KXK12963.1, ECO:0000313|Proteomes:UP000070321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB14 {ECO:0000313|EMBL:KXK12963.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK12963.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMZR01000047; KXK12963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KUG0; -.
DR   STRING; 1617415.UZ14_CFX002002009; -.
DR   Proteomes; UP000070321; 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; 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:KXK12963.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          5..223
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   288 AA;  31638 MW;  784A0836C4958FC6 CRC64;
     MRSRRALLYM PGDNWKMITK SITLGVDSIC MDMEDGTAVN KKQEARETIA KALQELNFGE
     SEKLARINSI GSGWEKDDIE SVLPYQPDGI VIPKVESVEQ IEWASKIIES AELKHGWKVN
     SIRILIGIET AKGILNLKEI ASHPRLDAMI FGGEDFAASI GAKRTKDAIE LLYARQAVIV
     ACAANDLQAI DIVTIDYKDA ELLKAESAFG ARLGFSGKQI IHPNQVSAVQ EAFTPSDEEI
     AYAKRIVETF EASQKEGKGA YSLDGKMIDM PLLKNAQKVL ARAKVASK
//