ID   A0A1H8CS28_9PROT        Unreviewed;       315 AA.
AC   A0A1H8CS28;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Beta-methylmalyl-CoA/L-malyl-CoA lyase {ECO:0000313|EMBL:SEM97672.1};
GN   ORFNames=SAMN05216325_105105 {ECO:0000313|EMBL:SEM97672.1};
OS   Nitrosomonas marina.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=917 {ECO:0000313|EMBL:SEM97672.1, ECO:0000313|Proteomes:UP000199459};
RN   [1] {ECO:0000313|EMBL:SEM97672.1, ECO:0000313|Proteomes:UP000199459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm22 {ECO:0000313|EMBL:SEM97672.1,
RC   ECO:0000313|Proteomes:UP000199459};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOCP01000005; SEM97672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8CS28; -.
DR   STRING; 917.SAMN05216326_13716; -.
DR   OrthoDB; 348111at2; -.
DR   Proteomes; UP000199459; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:SEM97672.1};
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          19..248
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   315 AA;  34074 MW;  9AAA2A6488AF92E1 CRC64;
     MSHTLYETKT QRVQRCELAV PGSSPEMFEK ALKSGVDFVF LDLEDAVAPD DKLQARKNVI
     QAINDLDWKG HGVTVSVRIN GLDTQFMVRD VVDLVEQAGD KINTLLIPKV GVYADVYMVE
     AMVSQLEMQQ GLKNRIGLEA LIETALGMAN VEDIACNGSR GRLEALHFGV ADYAASNRAR
     TTNIGGLNPD YPGDQWHFAI SRMTVACRAY GLRPIDGPFG DIKDPEGYKL AARRAAALGC
     EGKWAIHPTQ IALANEVFTP PEAEVEKAKR ILAALKDAAA QGKGAAALDG RLIDAASERM
     ASNVVRIAEA IAAKK
//