(data stored in ACNUC7421 zone)

SWISSPROT: D4YXZ7_SPHJU

ID   D4YXZ7_SPHJU            Unreviewed;       391 AA.
AC   D4YXZ7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 41.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:BAI95229.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:BAI95229.1};
GN   Name=fadA {ECO:0000313|EMBL:BAI95229.1};
GN   OrderedLocusNames=SJA_C1-03950 {ECO:0000313|EMBL:BAI95229.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95229.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95229.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- SIMILARITY: Belongs to the thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; AP010803; BAI95229.1; -; Genomic_DNA.
DR   RefSeq; WP_013039011.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-03950; -.
DR   EnsemblBacteria; BAI95229; BAI95229; SJA_C1-03950.
DR   GeneID; 29272082; -.
DR   KEGG; sjp:SJA_C1-03950; -.
DR   eggNOG; ENOG4105CHU; Bacteria.
DR   eggNOG; COG0183; LUCA.
DR   HOGENOM; HOG000012239; -.
DR   KO; K00626; -.
DR   OMA; MTQIPIS; -.
DR   OrthoDB; POG091H086Y; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXZ7.
DR   SWISS-2DPAGE; D4YXZ7.
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:BAI95229.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:BAI95229.1}.
FT   DOMAIN        5    260       Thiolase_N. {ECO:0000259|Pfam:PF00108}.
FT   DOMAIN      268    389       Thiolase_C. {ECO:0000259|Pfam:PF02803}.
FT   ACT_SITE     89     89       Acyl-thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000429-1}.
FT   ACT_SITE    347    347       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
FT   ACT_SITE    377    377       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
SQ   SEQUENCE   391 AA;  40586 MW;  8874F6E5C49A2E47 CRC64;
     MPEAYIVSAR RTAGGRRNGR LAGWHPADLG ALVLDALVAD AGVDPAAIDD VIIGCVSQVG
     EQTFAFGRNI VLASSLPDSV PAVTIDRQCG SSQQAVHFAA QAVMSGLQDI VIAGGVESMT
     RVPMGSPITL AKAGGIGANP FSEAIQKRYG VEMFSQFHGA QMIADKYGFT RDDHDRFALA
     SHRKAAAAMN AGAFDAEIVP VPVVTAEGEQ AIHDRDEGVR ADASMESIGS VKLLSEGGTL
     SAATASQICD GASGVLVASE AAVRAHGLKP IARIVNLAVT AGDPVIMLEE PIPATRRVLD
     RAGMTMKDID LFEVNEAFAS IPMAWMKALD ADPERLNVNG GAIALGHPLG ATGTKLMATL
     IHALKARGQR YGLQTMCEGG GIANASIIEV L
//

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