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Database: UniProt
Entry: A0A1H3HYL0_9RHOB
LinkDB: A0A1H3HYL0_9RHOB
Original site: A0A1H3HYL0_9RHOB 
ID   A0A1H3HYL0_9RHOB        Unreviewed;       319 AA.
AC   A0A1H3HYL0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Beta-methylmalyl-CoA/L-malyl-CoA lyase {ECO:0000313|EMBL:SDY19874.1};
GN   ORFNames=SAMN05444340_104212 {ECO:0000313|EMBL:SDY19874.1};
OS   Citreimonas salinaria.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Citreimonas.
OX   NCBI_TaxID=321339 {ECO:0000313|EMBL:SDY19874.1, ECO:0000313|Proteomes:UP000199286};
RN   [1] {ECO:0000313|EMBL:SDY19874.1, ECO:0000313|Proteomes:UP000199286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26880 {ECO:0000313|EMBL:SDY19874.1,
RC   ECO:0000313|Proteomes:UP000199286};
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};
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; FNPF01000004; SDY19874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3HYL0; -.
DR   STRING; 321339.SAMN05444340_104212; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000199286; 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   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SDY19874.1};
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:UP000199286}.
FT   DOMAIN          15..253
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   319 AA;  34367 MW;  B16336F36A9A0E15 CRC64;
     MSFRIQPQPP ARPNRCQLFG PGSRPAIFEK MAKSEADVIN LDLEDSVSPD DKPGARANIV
     QAIGDIDWGA KTLSVRINGL DTPYWYRDVI DLLEQAGERL DQIMIPKVGC AADLYAVDAL
     VTAVEAAKGR KKRIAFEVII ESAAGIAHVQ EIAAASPRLQ AMSLGAADFA ASMGMATTGI
     GGTQENYYML HEGQKHWSDP WHWAQAAIVA ACRTHGVLPV DGPFGDFSDD DGFRAQALRS
     ATLGMVGKWA IHPKQVALAN EVFTPSDTAV AEAREILDAM EQAKARGEGA TVYKGRLVDI
     ASIKQAEVIV KQSEMIAAR
//
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