(data stored in SCRATCH zone)

SWISSPROT: Q2IMC3_ANADE

ID   Q2IMC3_ANADE            Unreviewed;       297 AA.
AC   Q2IMC3;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:ABC79958.1};
DE            EC=4.1.3.34 {ECO:0000313|EMBL:ABC79958.1};
GN   OrderedLocusNames=Adeh_0181 {ECO:0000313|EMBL:ABC79958.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79958.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|SAAS:SAAS00571010}.
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DR   EMBL; CP000251; ABC79958.1; -; Genomic_DNA.
DR   RefSeq; WP_011419241.1; NC_007760.1.
DR   STRING; 290397.Adeh_0181; -.
DR   EnsemblBacteria; ABC79958; ABC79958; Adeh_0181.
DR   KEGG; ade:Adeh_0181; -.
DR   eggNOG; ENOG4105CI0; Bacteria.
DR   eggNOG; COG2301; LUCA.
DR   HOGENOM; HOG000242281; -.
DR   KO; K01644; -.
DR   OMA; GVYNAFK; -.
DR   BioCyc; ADEH290397:G1G5W-187-MONOMER; -.
DR   Proteomes; UP000001935; 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; -; 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   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMC3.
DR   SWISS-2DPAGE; Q2IMC3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Lyase {ECO:0000313|EMBL:ABC79958.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2,
KW   ECO:0000256|SAAS:SAAS00460587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   DOMAIN        8    222       HpcH_HpaI. {ECO:0000259|Pfam:PF03328}.
FT   METAL       127    127       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   METAL       154    154       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   BINDING      69     69       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
FT   BINDING     127    127       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
SQ   SEQUENCE   297 AA;  30082 MW;  D3AEEE0B6B986C48 CRC64;
     MPVVRPRRSA LYLPGSNARA IEKARTLPAD ALILDLEDAV APAAKDAARA QVVAALAQGG
     FGRRERVVRV NGLGTPWGAA DLAALARAGA DAICLPKVER AAEVHAAVQA LAAGHAPAGL
     ALWCMIETPR GVLAAGEIAG ASPRVACLVA GTSDLVKDLG ARHTAGRAEV LTSLSLVLLA
     ARAHGLAALD GVFLDLEDAA GLEAACRQGR DLGFDGKTLI HPKQLEPANR AFAPDAEELG
     RARRVIAAHA EAEAAGLGVT VVDGRLVEAL HVEAARRTVA LAEAIAAGPG GAGPHAG
//

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