(data stored in SCRATCH zone)

SWISSPROT: Q3IDT0_PSEHT

ID   Q3IDT0_PSEHT            Unreviewed;       154 AA.
AC   Q3IDT0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 65.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|RuleBase:RU364072};
GN   Name=accB {ECO:0000313|EMBL:CAI85364.1};
GN   OrderedLocusNames=PSHAa0265 {ECO:0000313|EMBL:CAI85364.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85364.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85364.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000256|RuleBase:RU364072}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|RuleBase:RU364072}.
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DR   EMBL; CR954246; CAI85364.1; -; Genomic_DNA.
DR   RefSeq; WP_011326978.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDT0; -.
DR   STRING; 326442.PSHAa0265; -.
DR   EnsemblBacteria; CAI85364; CAI85364; PSHAa0265.
DR   KEGG; pha:PSHAa0265; -.
DR   PATRIC; fig|326442.8.peg.252; -.
DR   eggNOG; ENOG4105KM4; Bacteria.
DR   eggNOG; COG0511; LUCA.
DR   HOGENOM; HOG000008875; -.
DR   KO; K02160; -.
DR   OMA; IKSPIIG; -.
DR   OrthoDB; POG091H05PV; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR00531; BCCP; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   4: Predicted;
DR   PRODOM; Q3IDT0.
DR   SWISS-2DPAGE; Q3IDT0.
KW   Biotin {ECO:0000256|RuleBase:RU364072};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN       78    154       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   154 AA;  16157 MW;  B867DD97736B4BB5 CRC64;
     MDIRKIKKLI ELVEESGIAE LEITEGEESV RINRNNMSAG PGYAQFAPQQ YAPAPVAAPV
     AAAPAAAVEA AAPAASTGHQ VKSPMVGSFY AAASPEAPAY VEVGSQVKVG DTLCIIEAMK
     MMNQIESDKA GTVKAILAEN GEPIEFDQPL FIIE
//

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