BIOF_EMENI
ID BIOF_EMENI Reviewed; 412 AA.
AC C8V1D1;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000303|PubMed:20713166};
DE Short=AONS {ECO:0000303|PubMed:20713166};
DE EC=2.3.1.47 {ECO:0000305|PubMed:20713166};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000303|PubMed:20713166};
DE Short=7-KAP synthase {ECO:0000303|PubMed:20713166};
DE Short=KAPA synthase {ECO:0000303|PubMed:20713166};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000303|PubMed:20713166};
GN Name=bioF {ECO:0000303|PubMed:20713166}; ORFNames=ANIA_06645;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=20713166; DOI=10.1016/j.fgb.2010.08.004;
RA Magliano P., Flipphi M., Sanglard D., Poirier Y.;
RT "Characterization of the Aspergillus nidulans biotin biosynthetic gene
RT cluster and use of the bioDA gene as a new transformation marker.";
RL Fungal Genet. Biol. 48:208-215(2011).
CC -!- FUNCTION: 8-amino-7-oxononanoate synthase; part of the cluster involved
CC in the biosynthesis of biotin (also known as vitamin B8 or vitamin H),
CC a water-soluble vitamin that functions as a prosthetic group of many
CC carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase
CC (PubMed:20713166). Catalyzes the decarboxylative condensation of
CC pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-
CC oxononanoate (AON) (By similarity). {ECO:0000250|UniProtKB:B7LC58,
CC ECO:0000269|PubMed:20713166}.
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;
CC Evidence={ECO:0000305|PubMed:20713166};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:B7LC58};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000269|PubMed:20713166}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B7LC58}.
CC -!- INDUCTION: Expression is increased when transferring biotin auxotrophic
CC mutant mycelia from biotin-supplemented medium to biotin-deficient
CC medium. {ECO:0000269|PubMed:20713166}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000305}.
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DR EMBL; BN001301; CBF71163.1; -; Genomic_DNA.
DR AlphaFoldDB; C8V1D1; -.
DR SMR; C8V1D1; -.
DR STRING; 162425.CADANIAP00007427; -.
DR EnsemblFungi; CBF71163; CBF71163; ANIA_06645.
DR VEuPathDB; FungiDB:AN6645; -.
DR eggNOG; KOG1360; Eukaryota.
DR HOGENOM; CLU_015846_3_0_1; -.
DR InParanoid; C8V1D1; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 930001at2759; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000560; Chromosome I.
DR GO; GO:0005777; C:peroxisome; IMP:AspGD.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IMP:AspGD.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
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.
PE 2: Evidence at transcript level;
KW Biotin biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..412
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000449414"
FT BINDING 106..107
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:B7LC58"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B7LC58"
FT BINDING 187
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:B7LC58"
FT BINDING 219
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:B7LC58"
FT BINDING 247
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:B7LC58"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B7LC58"
FT MOD_RES 250
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:B7LC58"
SQ SEQUENCE 412 AA; 45580 MW; F24A828DD0587550 CRC64;
MGDSPKCLRD SLREALRRRE DKLCRRKLTI LPSSSVDFSS NDFLSLSTSP AYRARFLDIL
QQAPPLHPFA SGGSRLLDGN SAYAEELENF IAAFHNAPSG LLFNSGYDAN VGVFSSIPQP
GDLIVYDELI HASAHEGMRL SRAGKRIKFP HSSPDGLRAV LQAEITADPR LLQGRRNVFI
AFESVYSMDG DVAPIREFVE IVDQLLPYGN GYFLVDEAHA TGVFGPRGSG VVQELGLEDR
MFVRVHTFGK ALASHGAIVL CCADTRDYLI NYARSLIYTT ALGFPFLASI RAAYELLVEG
KTEQLQHKLG QLIAHFRTGL DNLNHKDSST FEVEHFTNSP IFSLRSSVPR VLASVCQEQG
YTVRAIMPPT VPAGKERVRV CLHAGNTVEE VDGLLETIAT WLQRMEKQKA RL
