ID   A0A159Z673_9RHOB        Unreviewed;       318 AA.
AC   A0A159Z673;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Citrate-lyase {ECO:0000313|EMBL:AMY70822.1};
GN   ORFNames=AKL17_3598 {ECO:0000313|EMBL:AMY70822.1};
OS   Frigidibacter mobilis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Frigidibacter.
OX   NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY70822.1, ECO:0000313|Proteomes:UP000076128};
RN   [1] {ECO:0000313|EMBL:AMY70822.1, ECO:0000313|Proteomes:UP000076128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA   Geng S., Pan X., Wu X.;
RT   "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT   oilfield in Xinjiang.";
RL   Submitted (SEP-2015) 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; CP012661; AMY70822.1; -; Genomic_DNA.
DR   RefSeq; WP_066815468.1; NZ_CP012661.1.
DR   AlphaFoldDB; A0A159Z673; -.
DR   STRING; 1335048.AKL17_3598; -.
DR   KEGG; daa:AKL17_3598; -.
DR   PATRIC; fig|1335048.3.peg.3732; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000076128; Chromosome.
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:AMY70822.1};
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          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   318 AA;  34205 MW;  18025F5E83585F7F CRC64;
     MSFRIQPAAP ARPNRCQLFG PGSRPAIFEK MATGAADVIN LDLEDSVSPA DKPQARSNII
     EAINDIDWGS KYLSVRINGL DTPFWYRDVV EILEQAGNRI DQIMIPKVGC AADVYAVDAL
     VTAIERAKGR TKPISFEVII ESAAGIAHVE EIAASSPRLQ AMSLGAADFA ASMGMQTTGI
     GGTQENYYML HEGARHWSDP WHWAQAAIVA ACRTHGVLPV DGPFGDFSDD EGFRAQARRS
     ATLGMVGKWA IHPKQVAIAN EVFTPSAEAV AEAREILAAM EAAKARGEGA TVYKGRLVDI
     ASIKQAEVIV RQSEMISG
//