ID Q6NID2_CORDI Unreviewed; 277 AA.
AC Q6NID2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Citrate lyase {ECO:0000313|EMBL:CAE49361.1};
GN OrderedLocusNames=DIP0845 {ECO:0000313|EMBL:CAE49361.1};
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE49361.1, ECO:0000313|Proteomes:UP000002198};
RN [1] {ECO:0000313|EMBL:CAE49361.1, ECO:0000313|Proteomes:UP000002198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC {ECO:0000313|Proteomes:UP000002198};
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; BX248356; CAE49361.1; -; Genomic_DNA.
DR RefSeq; WP_010934611.1; NC_002935.2.
DR AlphaFoldDB; Q6NID2; -.
DR STRING; 257309.DIP0845; -.
DR KEGG; cdi:DIP0845; -.
DR HOGENOM; CLU_044864_2_1_11; -.
DR Proteomes; UP000002198; 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; 2.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:CAE49361.1};
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:UP000002198}.
FT DOMAIN 12..96
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT DOMAIN 107..217
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 277 AA; 30228 MW; D17E9A935C3E93AF CRC64;
MTNRELILRP AVLFAPANRP EIIPKAAARA DMVILDLEDG AGSIDRNQAY ANIRNAGLDP
TTTFVRIVGP EDPHHAADLA FVKTTEYYNV IVPKIGAALP EGLDGLNVVP IIETPLAVIN
IASIAADPHV VGLYWGADDL TIALGGLYSR RRIDEPQPSS YRAPIEYARV QTLLHAAANG
KWALDAVYQD FKDLDGLYTE ALDSARMGFA AYPCIHPNQV DAVRRAFAPS AEQLEWAQRI
AEETKKHPGA FQLDGEMVDT PLIALAHRLL QRHAAVD
//
