(data stored in ACNUC7421 zone)

SWISSPROT: Q47T38_THEFY

ID   Q47T38_THEFY            Unreviewed;       318 AA.
AC   Q47T38;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   SubName: Full=Citryl-CoA lyase {ECO:0000313|EMBL:AAZ54379.1};
DE            EC=4.1.3.34 {ECO:0000313|EMBL:AAZ54379.1};
GN   OrderedLocusNames=Tfu_0341 {ECO:0000313|EMBL:AAZ54379.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54379.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|SAAS:SAAS00571010}.
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DR   EMBL; CP000088; AAZ54379.1; -; Genomic_DNA.
DR   RefSeq; WP_011290788.1; NC_007333.1.
DR   STRING; 269800.Tfu_0341; -.
DR   EnsemblBacteria; AAZ54379; AAZ54379; Tfu_0341.
DR   KEGG; tfu:Tfu_0341; -.
DR   eggNOG; ENOG4105CI0; Bacteria.
DR   eggNOG; COG2301; LUCA.
DR   HOGENOM; HOG000242281; -.
DR   KO; K01644; -.
DR   OMA; GVYNAFK; -.
DR   OrthoDB; 1107373at2; -.
DR   BioCyc; TFUS269800:G1G4Q-343-MONOMER; -.
DR   Proteomes; UP000000434; 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; Q47T38.
DR   SWISS-2DPAGE; Q47T38.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Lyase {ECO:0000313|EMBL:AAZ54379.1};
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:UP000000434}.
FT   DOMAIN       10    241       HpcH_HpaI. {ECO:0000259|Pfam:PF03328}.
FT   METAL       137    137       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   METAL       164    164       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   BINDING      71     71       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
FT   BINDING     137    137       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
SQ   SEQUENCE   318 AA;  34507 MW;  A7CF451F35FDDB05 CRC64;
     MNAVASRSRR SVLAVPASNP RFIEKARGLA VDAFFLDLED AVAPSEKERA REAAVAALNE
     GGWDGKVRTV RINDATTAWA YRDVITVVEG AGAALDCLVL PKVTGPAPIL WLDTLLTQIE
     RAVGLEVGRI GIEAQIEDAR GLTRINEIAA ASPRVETLVY GPADFMASIN MKTLTVGEQP
     PGYDVGDAYH YVLMRILTAA RAHDLQAIDG PYLKIRDVDG FTRAARRTAA LGFDGKWVLH
     PGQVDAANEV YAPTQEDYDH AELVLDAYDY ATRVQRRGAV MLGDEMLDEA SRKMALVIAA
     KGRAAGMKRT KTFVPDTE
//

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