ID BIOA_ECOLI STANDARD; PRT; 429 AA.
AC P12995;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 07-FEB-2006, entry version 64.
DE Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
DE (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA
DE aminotransferase).
GN Name=bioA; OrderedLocusNames=b0774;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=89066784; PubMed=3058702;
RA Otsuka A.J., Buoncristiani M.R., Howard P.K., Flamm J., Johnson O.,
RA Yamamoto R., Uchida K., Cook C., Ruppert J., Matsuzaki J.;
RT "The Escherichia coli biotin biosynthetic enzyme sequences predicted
RT from the nucleotide sequence of the bio operon.";
RL J. Biol. Chem. 263:19577-19585(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pearson B.M., McKee R.A.;
RT "Genetic material for expression of biotin synthetase enzymes.";
RL Patent number GB2216530, 11-OCT-1989.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX MEDLINE=99384134; PubMed=10452893; DOI=10.1006/jmbi.1999.2997;
RA Kack H., Sandmark J., Gibson K., Schneider G., Lindqvist Y.;
RT "Crystal structure of diaminopelargonic acid synthase: evolutionary
RT relationships between pyridoxal-5'-phosphate-dependent enzymes.";
RL J. Mol. Biol. 291:857-876(1999).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
CC oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
CC diaminononanoate.
CC -!- COFACTOR: Pyridoxal phosphate.
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
CC 6-carboxyhexanoyl-CoA: step 2.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family.
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DR EMBL; J04423; AAA23514.1; -; Genomic_DNA.
DR EMBL; A11524; CAA00964.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC73861.1; -; Genomic_DNA.
DR PIR; F64813; XNECDP.
DR PDB; 1DTY; X-ray; A/B=1-429.
DR PDB; 1MGV; X-ray; A/B=1-429.
DR PDB; 1MLY; X-ray; A/B=1-429.
DR PDB; 1MLZ; X-ray; A/B=1-429.
DR PDB; 1QJ3; X-ray; A/B=1-429.
DR PDB; 1QJ5; X-ray; A/B=1-429.
DR PDB; 1S06; X-ray; A/B=1-429.
DR PDB; 1S07; X-ray; A/B=1-429.
DR PDB; 1S08; X-ray; A/B=1-429.
DR PDB; 1S09; X-ray; A/B=1-429.
DR PDB; 1S0A; X-ray; A/B=1-429.
DR EchoBASE; EB0115; -.
DR EcoGene; EG10117; bioA.
DR BioCyc; EcoCyc:DAPASYN-MONOMER; -.
DR GO; GO:0005515; F:protein binding; IPI.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR005815; BioA.
DR PANTHER; PTHR11986; Aminotrans_3; 1.
DR PANTHER; PTHR11986:SF14; BioA; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
KW 3D-structure; Aminotransferase; Biotin biosynthesis;
KW Complete proteome; Pyridoxal phosphate; Transferase.
FT CHAIN 1 429 Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase.
FT /FTId=PRO_0000120366.
FT BINDING 274 274 Pyridoxal phosphate (covalent).
FT CONFLICT 11 11 R -> P (in Ref. 2).
FT CONFLICT 99 102 TPQP -> SGRNA (in Ref. 1).
FT HELIX 3 12
FT STRAND 13 13
FT TURN 16 17
FT STRAND 27 34
FT TURN 35 35
FT STRAND 36 39
FT TURN 40 41
FT STRAND 44 47
FT TURN 50 54
FT TURN 56 57
FT STRAND 59 59
FT HELIX 62 74
FT STRAND 83 84
FT HELIX 86 98
FT TURN 101 102
FT STRAND 103 109
FT HELIX 112 129
FT TURN 130 131
FT STRAND 136 140
FT TURN 141 142
FT HELIX 149 152
FT TURN 153 154
FT TURN 157 161
FT HELIX 162 165
FT TURN 166 168
FT STRAND 173 175
FT STRAND 181 181
FT HELIX 188 191
FT HELIX 192 201
FT TURN 202 204
FT STRAND 205 210
FT STRAND 214 215
FT TURN 217 219
FT STRAND 221 223
FT TURN 225 225
FT HELIX 226 238
FT TURN 239 239
FT STRAND 241 245
FT TURN 247 254
FT HELIX 259 263
FT TURN 264 264
FT STRAND 269 272
FT HELIX 274 277
FT TURN 278 279
FT STRAND 284 289
FT HELIX 290 297
FT TURN 298 298
FT TURN 300 301
FT TURN 309 312
FT HELIX 314 328
FT TURN 329 329
FT HELIX 331 347
FT HELIX 348 352
FT TURN 354 355
FT STRAND 356 362
FT TURN 363 364
FT STRAND 365 370
FT STRAND 374 374
FT HELIX 376 385
FT TURN 386 387
FT STRAND 388 389
FT STRAND 393 393
FT TURN 394 395
FT STRAND 396 399
FT TURN 403 404
FT HELIX 407 420
FT TURN 421 421
FT HELIX 424 426
FT STRAND 427 427
SQ SEQUENCE 429 AA; 47336 MW; 84D2D1AE3A1280FF CRC64;
MTTDDLAFDQ RHIWHPYTSM TSPLPVYPVV SAEGCELILS DGRRLVDGMS SWWAAIHGYN
HPQLNAAMKS QIDAMSHVMF GGITHAPAIE LCRKLVAMTP QPLECVFLAD SGSVAVEVAM
KMALQYWQAK GEARQRFLTF RNGYHGDTFG AMSVCDPDNS MHSLWKGYLP ENLFAPAPQS
RMDGEWDERD MVGFARLMAA HRHEIAAVII EPIVQGAGGM RMYHPEWLKR IRKICDREGI
LLIADEIATG FGRTGKLFAC EHAEIAPDIL CLGKALTGGT MTLSATLTTR EVAETISNGE
AGCFMHGPTF MGNPLACAAA NASLAILESG DWQQQVADIE VQLREQLAPA RDAEMVADVR
VLGAIGVVET THPVNMAALQ KFFVEQGVWI RPFGKLIYLM PPYIILPQQL QRLTAAVNRA
VQDETFFCQ
//