ID A0A087N4E0_9BACI Unreviewed; 294 AA.
AC A0A087N4E0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN ORFNames=CH76_03290 {ECO:0000313|EMBL:KFL43993.1};
OS Lysinibacillus sp. BF-4.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL43993.1, ECO:0000313|Proteomes:UP000029097};
RN [1] {ECO:0000313|EMBL:KFL43993.1, ECO:0000313|Proteomes:UP000029097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL43993.1,
RC ECO:0000313|Proteomes:UP000029097};
RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H.,
RA Grass G.;
RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus isolated
RT during an anthrax outbreak in Bavaria.";
RL Submitted (MAR-2014) 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:KFL43993.1}.
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DR EMBL; JPUW01000004; KFL43993.1; -; Genomic_DNA.
DR RefSeq; WP_036142891.1; NZ_JPUW01000004.1.
DR AlphaFoldDB; A0A087N4E0; -.
DR eggNOG; COG2301; Bacteria.
DR OrthoDB; 9786940at2; -.
DR Proteomes; UP000029097; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:SF10; CITRATE LYASE SUBUNIT BETA; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000029097}.
FT DOMAIN 6..225
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
SQ SEQUENCE 294 AA; 32170 MW; E68DF493F425A561 CRC64;
MKWQYRSMLF IPGVKDIWLA KLNENVADAI IMDLEDSVPQ ERKAQARDFV AQALNMPTKK
SLWVRINKTT QGYALEDIEA IVCAKLTGIV VPKVASVADV ISLSAQLAQV EQARGLAVGS
IRLLPMLETA QALWFAYDIA SIPRVAGIAG ISSKNGDAER SLGTRWTEEG LETLYLKSRT
VMAARAAGKM PIGGLWQNVH DLDGLTKAAS FNRQLGYDGE LILHPSNAPI VNQAYAPTLT
DIAYYEGMIA AFEQGKQQGV TAMLYEGEHI DYAHVETAKE IVAYAKKMLE GDAI
//
