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
//