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
//