ID B1ZHI1_METPB Unreviewed; 324 AA.
AC B1ZHI1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:ACB79917.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:ACB79917.1};
GN OrderedLocusNames=Mpop_1754 {ECO:0000313|EMBL:ACB79917.1};
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620 {ECO:0000313|EMBL:ACB79917.1, ECO:0000313|Proteomes:UP000007136};
RN [1] {ECO:0000313|EMBL:ACB79917.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJ001 {ECO:0000313|EMBL:ACB79917.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001029; ACB79917.1; -; Genomic_DNA.
DR RefSeq; WP_012453663.1; NC_010725.1.
DR AlphaFoldDB; B1ZHI1; -.
DR STRING; 441620.Mpop_1754; -.
DR KEGG; mpo:Mpop_1754; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_5; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000007136; Chromosome.
DR GO; GO:0008815; F:citrate (pro-3S)-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:ACB79917.1};
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 16..258
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 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 324 AA; 35506 MW; CAF4FAE21277685B CRC64;
MSFTLIQQAT PRLHRSELAV PGSNPTFMEK SAASKADVIF LDLEDAVAPD DKEQARKNII
QALNDLDWGN KTMMIRINGL DTHYMYRDVV DIVEACPRLD MILIPKVGVP ADVYAIDVLT
TQIEQAKKRE KKIGFEVLIE TALGMANVEA IATSSKRLEA MSFGVADYAA STRARSTVIG
GVNPDYSVLT DKDEAGNRET HWQDPWLFAQ NRMLVACRAY GLRPIDGPFG DFSDPDGYKS
AARRCAALGF EGKWAIHPSQ IDLANEVFTP SEAEVTKARR ILEAMEEAAK AGRGAVSLDG
RLIDIASIRM AEALIQKADA MGGK
//
