(data stored in SCRATCH917 zone)

HOGENOM: YERPD_1_PE1003

ID   YERPD_1_PE1003                       STANDARD;      PRT;   383 AA.
AC   YERPD_1_PE1003; D0JHQ8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=8-amino-7-oxononanoate synthase; Short=AONS; EC=2.3.1
DE   47;AltName: Full=7-keto-8-amino-pelargonic acid synthase;AltName:
DE   Full=8-amino-7-ketopelargonate synthase;AltName:
DE   Full=L-alanine--pimeloyl-CoA ligase; (YERPD_1.PE1003).
GN   Name=bioF; OrderedLocusNames=YPD4_1003;
OS   YERSINIA PESTIS D106004.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=637382;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS YERPD_1.PE1003.
CC       Yersinia pestis (strain D106004) chromosome, complete sequence.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D0JHQ8_YERPD
CC   -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-
CC       CoA and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC       coenzyme A, and carbon dioxide (By similarity).
CC   -!- CATALYTIC ACTIVITY: 6-carboxyhexanoyl-CoA + L-alanine = 8-amino-7-
CC       oxononanoate + CoA + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 8-amino-7-
CC       oxononanoate from pimeloyl-CoA: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. BioF subfamily.
CC   -!- GENE_FAMILY: HOG000221021 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D0JHQ8; -.
DR   EMBL; CP001585; ACY57912.1; -; Genomic_DNA.
DR   ProteinModelPortal; D0JHQ8; -.
DR   GenomeReviews; CP001585_GR; YPD4_1003.
DR   OMA; KDYASND; -.
DR   GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0016769; F:transferase activity, transferring nitrogenous groups; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01693; BioF_aminotrans_2; 1; -.
DR   InterPro; IPR022834; Amino_oxononanoate_synth.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004723; BioF.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   TIGRFAMs; TIGR00858; BioF; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR   HOGENOMDNA; YERPD_1.PE1003; -.
KW   ACY57912.100026476820036002503210000011;
KW   8-amino-7-oxononanoate synthase ;
KW   Biotin biosynthesis; Complete proteome; Pyridoxal phosphate;
KW   Transferase.
SQ   SEQUENCE   383 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSWQDKIAQG LQRRRDAAAY RTRQVNEGAN GRWLQSGERQ YLNFSSNDYL GLSQNDEVIA
     AWQQGARRYG VGSGGSGHVT GYSQPHARLE QQLADWLGYP RALLFISGYA ANQAVLTALT
     DADDRILADK LSHASLLEAA AHSPAQLRRF QHNQPEALQN LLIKPCQGQT LVVTEGVFSM
     DGDSAPLAAL QQQTSAAGGW LLVDDAHGIG VHGEGGRGSC WLQGVQPELL VVTFGKAFGL
     SGAAVLCQEP VAEYLLQYAR HLIYSTAMPP AQACALQAAL RQVQQGDALR QQLQQRIRQF
     RTAAAHLPLQ LGASKTAIQP LLVGDNQQSL IWAEQLRAAG LWVTAIRPPT VPPGSARLRI
     TLSAAHQPED IDRLLEVLYG LCH
//

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