BIOK_BACSU
ID BIOK_BACSU Reviewed; 448 AA.
AC P53555;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=L-Lysine--8-amino-7-oxononanoate transaminase {ECO:0000303|PubMed:15880481};
DE EC=2.6.1.105 {ECO:0000269|PubMed:15880481};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000305};
DE Short=DAPA AT;
DE Short=DAPA aminotransferase {ECO:0000303|PubMed:15880481};
DE AltName: Full=7,8-diaminononanoate synthase;
DE Short=DANS;
DE AltName: Full=Diaminopelargonic acid synthase;
DE AltName: Full=L-Lysine--8-amino-7-oxononanoate aminotransferase;
GN Name=bioK; Synonyms=bioA {ECO:0000303|PubMed:8763940};
GN OrderedLocusNames=BSU30230;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RX PubMed=8763940; DOI=10.1128/jb.178.14.4122-4130.1996;
RA Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J.;
RT "Cloning, sequencing, and characterization of the Bacillus subtilis biotin
RT biosynthetic operon.";
RL J. Bacteriol. 178:4122-4130(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION AS A LYSINE--8-AMINO-7-OXONONANOATE AMINOTRANSFERASE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=168 / PY79;
RX PubMed=15880481; DOI=10.1002/bit.20488;
RA Van Arsdell S.W., Perkins J.B., Yocum R.R., Luan L., Howitt C.L.,
RA Chatterjee N.P., Pero J.G.;
RT "Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA
RT utilizes lysine rather than S-adenosylmethionine as the amino donor in the
RT KAPA-to-DAPA reaction.";
RL Biotechnol. Bioeng. 91:75-83(2005).
RN [5] {ECO:0007744|PDB:3DOD, ECO:0007744|PDB:3DRD, ECO:0007744|PDB:3DU4}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE
RP AND 7-KETO-8-AMINOPELARGONIC ACID, COFACTOR, AND SUBUNIT.
RX PubMed=20565114; DOI=10.1021/bi902097j;
RA Dey S., Lane J.M., Lee R.E., Rubin E.J., Sacchettini J.C.;
RT "Structural characterization of the Mycobacterium tuberculosis biotin
RT biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin
RT synthetase.";
RL Biochemistry 49:6746-6760(2010).
CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from L-lysine
CC to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic
CC acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine
CC as an amino donor in the biosynthesis of DAPA.
CC {ECO:0000269|PubMed:15880481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + L-lysine = (7R,8S)-7,8-
CC diammoniononanoate + (S)-2-amino-6-oxohexanoate;
CC Xref=Rhea:RHEA:26329, ChEBI:CHEBI:32551, ChEBI:CHEBI:58321,
CC ChEBI:CHEBI:149468, ChEBI:CHEBI:149469; EC=2.6.1.105;
CC Evidence={ECO:0000269|PubMed:15880481};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15880481, ECO:0000269|PubMed:20565114};
CC -!- ACTIVITY REGULATION: Inhibited by 7-keto-8-aminopelargonic acid at
CC concentrations above 80 uM. {ECO:0000269|PubMed:15880481}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.6. {ECO:0000269|PubMed:15880481};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (Lys route).
CC {ECO:0000305|PubMed:15880481}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20565114}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000305}.
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DR EMBL; U51868; AAB17458.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00262.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15001.1; -; Genomic_DNA.
DR PIR; C69594; C69594.
DR RefSeq; NP_390901.1; NC_000964.3.
DR RefSeq; WP_004398913.1; NZ_JNCM01000036.1.
DR PDB; 3DOD; X-ray; 1.90 A; A/B=1-448.
DR PDB; 3DRD; X-ray; 2.17 A; A/B=1-448.
DR PDB; 3DU4; X-ray; 2.20 A; A/B=1-448.
DR PDB; 6WNN; X-ray; 2.59 A; A/B=1-448.
DR PDBsum; 3DOD; -.
DR PDBsum; 3DRD; -.
DR PDBsum; 3DU4; -.
DR PDBsum; 6WNN; -.
DR AlphaFoldDB; P53555; -.
DR SMR; P53555; -.
DR IntAct; P53555; 1.
DR MINT; P53555; -.
DR STRING; 224308.BSU30230; -.
DR PaxDb; P53555; -.
DR PRIDE; P53555; -.
DR EnsemblBacteria; CAB15001; CAB15001; BSU_30230.
DR GeneID; 936286; -.
DR KEGG; bsu:BSU30230; -.
DR PATRIC; fig|224308.179.peg.3279; -.
DR eggNOG; COG0161; Bacteria.
DR InParanoid; P53555; -.
DR OMA; VAVKMCL; -.
DR PhylomeDB; P53555; -.
DR BioCyc; BSUB:BSU30230-MON; -.
DR BioCyc; MetaCyc:BSU30230-MON; -.
DR BRENDA; 2.6.1.105; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Biotin biosynthesis; Cytoplasm;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..448
FT /note="L-Lysine--8-amino-7-oxononanoate transaminase"
FT /id="PRO_0000120361"
FT BINDING 113..114
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:20565114,
FT ECO:0007744|PDB:3DOD, ECO:0007744|PDB:3DU4"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20565114,
FT ECO:0007744|PDB:3DU4"
FT BINDING 251
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20565114,
FT ECO:0007744|PDB:3DU4"
FT BINDING 316..317
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:20565114,
FT ECO:0007744|PDB:3DOD, ECO:0007744|PDB:3DU4"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20565114,
FT ECO:0007744|PDB:3DU4"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:20565114,
FT ECO:0007744|PDB:3DOD, ECO:0007744|PDB:3DU4"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:3DU4"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3DU4"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3DU4"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3DU4"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6WNN"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 189..207
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:3DOD"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6WNN"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3DOD"
FT TURN 253..260
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3DOD"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 322..337
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 340..358
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:3DOD"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 394..404
FT /evidence="ECO:0007829|PDB:3DOD"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6WNN"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:3DOD"
FT HELIX 426..444
FT /evidence="ECO:0007829|PDB:3DOD"
SQ SEQUENCE 448 AA; 50112 MW; 38F104A93A74AA24 CRC64;
MTHDLIEKSK KHLWLPFTQM KDYDENPLII ESGTGIKVKD INGKEYYDGF SSVWLNVHGH
RKKELDDAIK KQLGKIAHST LLGMTNVPAT QLAETLIDIS PKKLTRVFYS DSGAEAMEIA
LKMAFQYWKN IGKPEKQKFI AMKNGYHGDT IGAVSVGSIE LFHHVYGPLM FESYKAPIPY
VYRSESGDPD ECRDQCLREL AQLLEEHHEE IAALSIESMV QGASGMIVMP EGYLAGVREL
CTTYDVLMIV DEVATGFGRT GKMFACEHEN VQPDLMAAGK GITGGYLPIA VTFATEDIYK
AFYDDYENLK TFFHGHSYTG NQLGCAVALE NLALFESENI VEQVAEKSKK LHFLLQDLHA
LPHVGDIRQL GFMCGAELVR SKETKEPYPA DRRIGYKVSL KMRELGMLTR PLGDVIAFLP
PLASTAEELS EMVAIMKQAI HEVTSLED
