ID   A0A1H1N2S4_9ACTN        Unreviewed;       362 AA.
AC   A0A1H1N2S4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Beta-methylmalyl-CoA/L-malyl-CoA lyase {ECO:0000313|EMBL:SDR93421.1};
GN   ORFNames=SAMN04488570_0755 {ECO:0000313|EMBL:SDR93421.1};
OS   Nocardioides scoriae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=642780 {ECO:0000313|EMBL:SDR93421.1, ECO:0000313|Proteomes:UP000198859};
RN   [1] {ECO:0000313|Proteomes:UP000198859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22127 {ECO:0000313|Proteomes:UP000198859};
RA   Varghese N., Submissions S.;
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; LT629757; SDR93421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1N2S4; -.
DR   STRING; 642780.SAMN04488570_0755; -.
DR   OrthoDB; 5172636at2; -.
DR   Proteomes; UP000198859; Chromosome i.
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:SDR93421.1};
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          30..199
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   362 AA;  39100 MW;  8D9FE27D7FE3BC7C CRC64;
     MRSAKDFFAP LAVGAPTPLR EIPTRPSRAI HFFDPSNPKM AAKVPDMVGS VDVLLGNLED
     AVKADNKLAA RQGLVEVARG TEGLGGPDSP TQLWTRVNAL DSPWGLDDLT TLVTEIGDRL
     DVVMVPKVQG AEDIHYVDRL LAQLEAKAGL DRPILVHAIL ETARGMVNVE EICGASPRMQ
     GLSLGPADLA ADRRMKTTRV GGGHPGYLVR QDPLSSSPED VARERATHQQ DLWHYTIARM
     VDACAMHGIF PYYGPFGDIA DVVACEDQFR NAFLLGCVGT WSLHPKQIAI AHRVFSPAPE
     DVAHARRVVE AMGDGTGAVM LDGKMEDDAS LKQCLVMVEL AEQLSAVDPE LKQRYDAIGT
     GA
//