ID A9CHD0_AGRFC Unreviewed; 294 AA.
AC A9CHD0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Citrate lyase, beta subunit {ECO:0000313|EMBL:AAK88501.1};
GN Name=citE {ECO:0000313|EMBL:AAK88501.1};
GN OrderedLocusNames=Atu2788 {ECO:0000313|EMBL:AAK88501.1};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK88501.1, ECO:0000313|Proteomes:UP000000813};
RN [1] {ECO:0000313|EMBL:AAK88501.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2] {ECO:0000313|EMBL:AAK88501.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK88501.1; -; Genomic_DNA.
DR PIR; AC2919; AC2919.
DR PIR; D97693; D97693.
DR RefSeq; NP_355716.1; NC_003062.2.
DR AlphaFoldDB; A9CHD0; -.
DR STRING; 176299.Atu2788; -.
DR EnsemblBacteria; AAK88501; AAK88501; Atu2788.
DR KEGG; atu:Atu2788; -.
DR PATRIC; fig|176299.10.peg.2798; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_5; -.
DR OrthoDB; 9800547at2; -.
DR PhylomeDB; A9CHD0; -.
DR BioCyc; AGRO:ATU2788-MONOMER; -.
DR Proteomes; UP000000813; Chromosome circular.
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:AAK88501.1};
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:UP000000813}.
FT DOMAIN 5..223
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 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 294 AA; 32328 MW; ADDD4BAD70C526CD CRC64;
MRPRRSLLSV PAINIRALEK IRELDCDGVI LDLEDSVAPD MKGKARENLE KLFSGPPFDG
RETIIRINPL STPDGKADLQ LVLSCRPDAV LLPKVEQPSD IHDVADFLAE ADAPEHLKIW
AMIETPLGVL NAASIADAAH TPNARLAAFV IGLNDLRKET HVPRLPGRTY LVPWMMQVIL
AARAYGLDVI DSVSNDFRDI EAFEAECEQG RAMGFDGKML IHPAQIEAAN RHFGPDEATL
AEARAIIAAF AKPESVELNI INMNGQMIER LHVGQAERLV AMADIIAQRK AKKT
//
