ID   A0A1M5BQH6_9BACE        Unreviewed;       295 AA.
AC   A0A1M5BQH6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SHF44675.1};
GN   ORFNames=SAMN05444349_12020 {ECO:0000313|EMBL:SHF44675.1};
OS   Bacteroides faecichinchillae.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=871325 {ECO:0000313|EMBL:SHF44675.1, ECO:0000313|Proteomes:UP000184436};
RN   [1] {ECO:0000313|EMBL:SHF44675.1, ECO:0000313|Proteomes:UP000184436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26883 {ECO:0000313|EMBL:SHF44675.1,
RC   ECO:0000313|Proteomes:UP000184436};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQVD01000020; SHF44675.1; -; Genomic_DNA.
DR   RefSeq; WP_073349938.1; NZ_SSTN01000039.1.
DR   AlphaFoldDB; A0A1M5BQH6; -.
DR   STRING; 871325.SAMN05444349_12020; -.
DR   OrthoDB; 9786940at2; -.
DR   Proteomes; UP000184436; 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:SF1; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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:SHF44675.1};
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:UP000184436}.
FT   DOMAIN          6..226
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         158
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   295 AA;  33161 MW;  0A95947F7F44757E CRC64;
     MEHLFRSLMF VPAHNERLMN SAAKSLADVL LLDIEDSVQP LQNKQIARDN IIRYVQSGVF
     KNRAIYPRIN DRESGELLKD IYQLTIPGIT GFMYPKSVKG EDIYFIGKLL ETVEYEKGYP
     IGTFKLIPLI ETTGAVMNIK DICMACTRVV AVAFGCEDYV TNLQGKHDSS GESIFAARSI
     IALSARACNV FPIDTVHIKV HDLDDLERNL ILSKKLGFEG MLVLNPKELP LVHQYYSPNE
     EEINWATEML ALSDTVVKEG KGVAVKDNKF IGPPMVKMAK NILDKRDLIV NQKNV
//