ID   U6SKY2_9BACI            Unreviewed;       295 AA.
AC   U6SKY2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN   ORFNames=A33I_20695 {ECO:0000313|EMBL:ERN51301.1};
OS   Alkalihalophilus marmarensis DSM 21297.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX   NCBI_TaxID=1188261 {ECO:0000313|EMBL:ERN51301.1, ECO:0000313|Proteomes:UP000017170};
RN   [1] {ECO:0000313|EMBL:ERN51301.1, ECO:0000313|Proteomes:UP000017170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21297 {ECO:0000313|EMBL:ERN51301.1,
RC   ECO:0000313|Proteomes:UP000017170};
RX   PubMed=24285666;
RA   Wernick D.G., Choi K.Y., Tat C.A., Lafontaine Rivera J.G., Liao J.C.;
RT   "Genome Sequence of the Extreme Obligate Alkaliphile Bacillus marmarensis
RT   Strain DSM 21297.";
RL   Genome Announc. 1:e00967-e00913(2013).
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:ERN51301.1}.
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DR   EMBL; ATAE01000065; ERN51301.1; -; Genomic_DNA.
DR   RefSeq; WP_022629843.1; NZ_ATAE01000065.1.
DR   AlphaFoldDB; U6SKY2; -.
DR   PATRIC; fig|1188261.3.peg.3858; -.
DR   Proteomes; UP000017170; 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: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   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          4..223
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   295 AA;  33317 MW;  CBBFE5C485BA749E CRC64;
     MLARSWLFVP GNRMKVIEKA ELLDADVIIY DLEDAVLLQD KIQAREMVIE ALQSSKKNIF
     VRMNSLSDMF GHEDVLSLLS NYNKSLKGLI LPKVSSAQQI KSLETMLITY EKKYNIHYEL
     EIVPLIESAA GVHFCFDIAS ASPRVKRLAF GAVDYCLDVN ITPTKCGNEL LYARSQIVNA
     SRAAEKLQPI DTVYIHFNDY EGLDIEINTA KGLGFGGKLV IHPNQIDEVN KKFAPTEEEV
     LDAKEILETV EQDGAAVFQL NGRMIDEPII KKARITLEKY RLIKGENPNL TWEKL
//