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Database: UniProt
Entry: A0A1H9XDD5_9PSEU
LinkDB: A0A1H9XDD5_9PSEU
Original site: A0A1H9XDD5_9PSEU 
ID   A0A1H9XDD5_9PSEU        Unreviewed;       354 AA.
AC   A0A1H9XDD5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Beta-methylmalyl-CoA/L-malyl-CoA lyase {ECO:0000313|EMBL:SES44200.1};
GN   ORFNames=SAMN04487818_114113 {ECO:0000313|EMBL:SES44200.1};
OS   Actinokineospora terrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=155974 {ECO:0000313|EMBL:SES44200.1, ECO:0000313|Proteomes:UP000199051};
RN   [1] {ECO:0000313|EMBL:SES44200.1, ECO:0000313|Proteomes:UP000199051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44260 {ECO:0000313|EMBL:SES44200.1,
RC   ECO:0000313|Proteomes:UP000199051};
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; FOGI01000014; SES44200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9XDD5; -.
DR   STRING; 155974.SAMN04487818_114113; -.
DR   Proteomes; UP000199051; 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:SES44200.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199051}.
FT   DOMAIN          29..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   354 AA;  38585 MW;  7E73174EDF239C09 CRC64;
     MRSPKDFFRP LAVGAPEPVR EIPFRPSRMI HFFDPSNEKM AAKVPDLLAK ADVVLGNLED
     AVRADRKVAA REGLVRVGRA TDFGDTQLWT RVNSLDSPWV LDDLITLVTE IGDKLDVIMV
     PKVESAADIH YVDRLLAQLE ARAGLTRPIL VHALLETAAG VANVEDIATA SPRMQGISLG
     PADLAASRRM KTTRVGGGHP GYLVRTDPLG DDLTTGRTTY QQDLWHYTVA RMVDACAAAG
     ILPYYGPFGD IADVVACEDQ FRNAFLLGCV GAWSLHPRQI EIARRVFSPD PAEVAWARRV
     IEAMGDGTGA VMLDGKMQDD ATVKQCRVMV ELADALAARD PELARAYSED ANRG
//
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