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BIOF_CELJU
ID   BIOF_CELJU              Reviewed;         398 AA.
AC   B3PI88;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE            Short=AONS {ECO:0000255|HAMAP-Rule:MF_01693};
DE            EC=2.3.1.47 {ECO:0000255|HAMAP-Rule:MF_01693};
DE   AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE            Short=7-KAP synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE            Short=KAPA synthase {ECO:0000255|HAMAP-Rule:MF_01693};
DE   AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000255|HAMAP-Rule:MF_01693};
GN   Name=bioF {ECO:0000255|HAMAP-Rule:MF_01693}; OrderedLocusNames=CJA_0427;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
CC   -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-
CC       carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC       [acyl-carrier protein], and carbon dioxide. {ECO:0000255|HAMAP-
CC       Rule:MF_01693}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-
CC         oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846,
CC         ChEBI:CHEBI:149468; EC=2.3.1.47; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01693};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01693};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01693}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01693}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. BioF subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01693}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACE83909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000934; ACE83909.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041550932.1; NC_010995.1.
DR   AlphaFoldDB; B3PI88; -.
DR   SMR; B3PI88; -.
DR   STRING; 498211.CJA_0427; -.
DR   EnsemblBacteria; ACE83909; ACE83909; CJA_0427.
DR   KEGG; cja:CJA_0427; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_2_6; -.
DR   OrthoDB; 479874at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01693; BioF_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004723; AONS_Archaea/Proteobacteria.
DR   InterPro; IPR022834; AONS_Proteobacteria.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00858; bioF; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..398
FT                   /note="8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000380951"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         110..111
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         181
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         209
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         238
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
FT   MOD_RES         241
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01693"
SQ   SEQUENCE   398 AA;  42668 MW;  F1A434281FA3CC65 CRC64;
     MPSHLDQTLA AALSERRAQY RYRQRKLLQS PQTPELVVDG KTYLAFCSND YLGLANHPQV
     IAAQQQAAAR WGAGSGASHL VAGHTQEHHA LEEELAAFTG RQRALLFSTG YMANLGVIST
     LVGQGDGVFE DRLNHASLLD GGLLSGARFQ RFLHSDINNL QARLRKTDAA RKLVVVDGVF
     SMDGDCAPLP QLAQVCAQEN AWLMVDDAHG FGVLGETGAG TCEHFGLDQQ QVPVLMGTLG
     KALGSFGAFV AGSETLIETL INFARPYIYT TAMPPPVAAA TRASLRLVQS EAWRRTHVQQ
     LIAQFRNGAQ DLGLQLMDSF SPVQPLLVGS EAKALAIAEA LAHRGILIIA IRPPTVPVGS
     SRLRITLSAA HTEAQVAQLL DVLGEVMNST AIRGLADD
 
 
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