ID A0A0T5ZSJ4_9BACT Unreviewed; 346 AA.
AC A0A0T5ZSJ4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Citrate (Pro-3S)-lyase, citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:KRT65788.1};
DE EC=4.1.3.34 {ECO:0000313|EMBL:KRT65788.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:KRT65788.1};
GN ORFNames=XU11_C0019G0009 {ECO:0000313|EMBL:KRT65788.1};
OS Candidatus Dadabacteria bacterium CSP1-2.
OC Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT65788.1, ECO:0000313|Proteomes:UP000051780};
RN [1] {ECO:0000313|EMBL:KRT65788.1, ECO:0000313|Proteomes:UP000051780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT65788.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-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:KRT65788.1}.
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DR EMBL; LDXN01000019; KRT65788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZSJ4; -.
DR STRING; 1640508.XU11_C0019G0009; -.
DR Proteomes; UP000051780; Unassembled WGS sequence.
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:SF0; 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:KRT65788.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 27..254
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 346 AA; 38863 MW; E67F80D65A9D9653 CRC64;
MFVLDEGKRV VVPRTELTYP GHNLKLHQSA ADTAKSPVDH VMADLEDACP YEFKGDKSRQ
VMVEALNTID FGKKVVTVRP NNLRSEFFYG DMEAVMSGAV DKFHGVIIPK IHGPEDIKLV
SDLLDELEAR YGWKTKVAIE SLIERPRALE YAYEIATASP RMAGLIFGIA DYTAELGGDP
DLLLDRQNEM FYYEKKAVVT AAKAAELHAV DNVYLRIWRK DDPPEVVKQI DEGLRRKNEV
AAAIGMDGTW VIHPQQAQIA NECFTPTKKQ IEEAKHQLDF YHEMGGGSMF DPKTGQMIDE
ATAKIALMRV SKAYMAGLVD KEYVDSMAEK SKSITGYDIR RAGERR
//
