ID   A0A1A8XI51_9PROT        Unreviewed;       359 AA.
AC   A0A1A8XI51;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:SBT04047.1};
GN   ORFNames=ACCAA_130031 {ECO:0000313|EMBL:SBT04047.1};
OS   Candidatus Accumulibacter aalborgensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1860102 {ECO:0000313|EMBL:SBT04047.1, ECO:0000313|Proteomes:UP000199169};
RN   [1] {ECO:0000313|EMBL:SBT04047.1, ECO:0000313|Proteomes:UP000199169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3 {ECO:0000313|EMBL:SBT04047.1};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; FLQX01000035; SBT04047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A8XI51; -.
DR   STRING; 1860102.ACCAA_130031; -.
DR   Proteomes; UP000199169; 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:UP000199169}.
FT   DOMAIN          50..194
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   359 AA;  39385 MW;  E99F26EF466D72D0 CRC64;
     MKLPVHFYKP LAIGAPQPLR ELPVRPERMI HFFPPHIDKI RAKAPETARQ CDAMCGNLED
     AIPIEAKDAA RAGFIDLLSK NDFGDTAMWV RINALNSPWV LDDLHEIIKH VGNKVDVIMI
     PKVEGPWDIH FVDQYVSLLE AKYAIKKPIL LHALLETAQG VTNVEAICGA SPRMHGLSLG
     PADLAASRGM KTTRVGGGHP GYGVLADPEA GQEEGQQRRA FFQQDLWHYT VARMVDAAVS
     HGLHAFYGPF GDLKDEAACE AQFRNAFLMG CSGAWSLAPN QIAIAKRVFS PDVKEVLFAK
     RILEAMPDGS GVATIDGKMQ DDATWKQAKV IVDLARLVAR RDPELAAAYG WSSSSHAQQ
//