ID M1MW20_9CLOT Unreviewed; 299 AA.
AC M1MW20;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:AGF55697.1};
DE EC=4.1.3.34 {ECO:0000313|EMBL:AGF55697.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:AGF55697.1};
GN Name=citE1 {ECO:0000313|EMBL:AGF55697.1};
GN ORFNames=Cspa_c19290 {ECO:0000313|EMBL:AGF55697.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF55697.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF55697.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) 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; CP004121; AGF55697.1; -; Genomic_DNA.
DR RefSeq; WP_015392018.1; NZ_AOIF01000124.1.
DR AlphaFoldDB; M1MW20; -.
DR KEGG; csr:Cspa_c19290; -.
DR PATRIC; fig|931276.5.peg.1919; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_2_9; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000011728; Chromosome.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
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:AGF55697.1};
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:UP000011728}.
FT DOMAIN 11..230
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 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 299 AA; 33839 MW; BDF4625D961C275E CRC64;
MIKKTLWGAH LFVPGNNAGF LCKLPIINVK NIIIDLEFAT KMPFKTDGRY LTRNAISYIR
SIRPDINICV RVNLSSAREL QDEDIKTVIQ AKPDSIRIPS VSNKYEVEYV DELLTKFEKE
NKMEIGSIKL HPMIENPQGL KHISDIIQAS NRVEAIALGG EDWAYNCGLH RTKEGHELEL
IKFEMVTVAA EYKILAIDTV FSFLDDTAGL ISDCKNSRIL GFRARSTINP RQLEIINNAY
APLNEEIEWA KSTLDDLTEV KFNNTINYVS KGVIVDPLAI YQAKDILNNI NEVNLNEVS
//
