(data stored in SCRATCH zone)

SWISSPROT: A1AZI1_PARDP

ID   A1AZI1_PARDP            Unreviewed;       279 AA.
AC   A1AZI1;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:ABL68675.1};
DE            EC=4.1.3.34 {ECO:0000313|EMBL:ABL68675.1};
GN   OrderedLocusNames=Pden_0563 {ECO:0000313|EMBL:ABL68675.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68675.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
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.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-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; CP000489; ABL68675.1; -; Genomic_DNA.
DR   RefSeq; WP_011746908.1; NC_008686.1.
DR   STRING; 318586.Pden_0563; -.
DR   PRIDE; A1AZI1; -.
DR   EnsemblBacteria; ABL68675; ABL68675; Pden_0563.
DR   KEGG; pde:Pden_0563; -.
DR   eggNOG; ENOG4105CI0; Bacteria.
DR   eggNOG; COG2301; LUCA.
DR   HOGENOM; HOG000242281; -.
DR   KO; K14451; -.
DR   OMA; GVYNAFK; -.
DR   BioCyc; PDEN318586:G1GW1-571-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZI1.
DR   SWISS-2DPAGE; A1AZI1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Lyase {ECO:0000313|EMBL:ABL68675.1};
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:UP000000361}.
FT   DOMAIN        6    211       HpcH_HpaI. {ECO:0000259|Pfam:PF03328}.
FT   METAL       117    117       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   METAL       143    143       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   BINDING      66     66       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
FT   BINDING     117    117       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
SQ   SEQUENCE   279 AA;  29730 MW;  CB50E889C107D592 CRC64;
     MTRPYRSVLY IPAANARAME KAQTLAADAI IFDLEDAVAP AEKVGARELL ARALQADYGG
     RARIVRINGM DTEWGEGDAR TFAAGADAVL VPKVSRGADL DRVAALVPDT PLWAMMETAE
     GMLNAAEIAA HPRLQGMVMG TNDLAKELNS RFRADRLPMM AGLGLCLLAA RAHGRVIVDG
     VFNAFKDEEG LRAECEQGRD MGFDGKTLIH PAQLAVANEV FAPSEAEVDL ARRQIEAFDE
     AQAQGKGVAV VDGRIVENLH VETARATLAK AAAIAELAG
//

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