ID A0A0B7ITK1_9PROT Unreviewed; 330 AA.
AC A0A0B7ITK1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:CEN55578.1};
GN ORFNames=BN1209_0533 {ECO:0000313|EMBL:CEN55578.1};
OS Candidatus Methylopumilus turicensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN55578.1, ECO:0000313|Proteomes:UP000056322};
RN [1] {ECO:0000313|Proteomes:UP000056322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000056322};
RA Salcher M.M.;
RL Submitted (DEC-2014) 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; LN794158; CEN55578.1; -; Genomic_DNA.
DR RefSeq; WP_045750827.1; NZ_LN794158.1.
DR AlphaFoldDB; A0A0B7ITK1; -.
DR STRING; 1581680.BN1209_0533; -.
DR KEGG; mbac:BN1209_0533; -.
DR HOGENOM; CLU_073837_0_0_4; -.
DR Proteomes; UP000056322; Chromosome 1.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.960; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR040186; Citramalyl-CoA_lyase.
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; PTHR11105:SF0; CITRAMALYL-COA LYASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11105; CITRATE LYASE SUBUNIT BETA-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|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000056322}.
FT DOMAIN 52..239
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 330 AA; 36660 MW; 0F7AF7DF0C0FC4B2 CRC64;
MNTLVHPNDA LFKGEKAFPV IPSCEHFAGS EKLILKALQI QDELGPIFDI TCDCEDGAAA
GQEREHAEMI VRVQQSQANK HKMAGVRIHD YTHPAWRQDV DIFVEGIGNL VAYITIPKST
NAAQVKEMIT YIQTKCKEHG IKREIPIHIL IETHGALHEV FEIAALPWIQ VLDFGLMDFV
SGHHGAIPAS AMRSPGQFEH RLLARAKSEV VAAALMHGIV PAHNVSLDLK NTVATNSDAS
RARQEFGFLR MWSIYPTQIQ AIVDAMKPNL DEVQDAADIL IAAQKAEWGP IQHAGELHDR
ATYRYYWEVL QKAKVSGISI PAEAEHAFFA
//