ID Q0AKN0_MARMM Unreviewed; 282 AA.
AC Q0AKN0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:ABI67163.1};
DE EC=4.1.3.34 {ECO:0000313|EMBL:ABI67163.1};
GN OrderedLocusNames=Mmar10_2882 {ECO:0000313|EMBL:ABI67163.1};
OS Maricaulis maris (strain MCS10).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI67163.1, ECO:0000313|Proteomes:UP000001964};
RN [1] {ECO:0000313|EMBL:ABI67163.1, ECO:0000313|Proteomes:UP000001964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI67163.1,
RC ECO:0000313|Proteomes:UP000001964};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) 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; CP000449; ABI67163.1; -; Genomic_DNA.
DR RefSeq; WP_011644807.1; NC_008347.1.
DR AlphaFoldDB; Q0AKN0; -.
DR STRING; 394221.Mmar10_2882; -.
DR KEGG; mmr:Mmar10_2882; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_5; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000001964; Chromosome.
DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
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:ABI67163.1};
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:UP000001964}.
FT DOMAIN 6..217
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 282 AA; 29851 MW; A7E94DD9E7E67424 CRC64;
MRRLIRSALF VPASKPRAIE KAAHVGADLL ILDLEDAVGP DEKGEARTAV DVAMHCWEAS
GSVRAVRVNA LDSEWGAADM RAAARADAIV LPKVEQVGDL HAARSALSSH GSSIPIWAMI
ETPRALLALN AISSAVGTGL AGLIAGTNDL CKELRCSPEH ERLALVPHLV NMVCAARARG
LYVLDGVYNH FKDPKGFRAE AEQGRALGFD GKSLIHPGQV DLAHLYFGPT ARDLEHAAKI
VAAFASPENA GKGVIALDGD MVERLHLEAA RALLSTASEN DS
//
