BIODA_EMENI
ID BIODA_EMENI Reviewed; 787 AA.
AC Q5AYI6; C8V1D0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Bifunctional dethiobiotin synthetase/adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000303|PubMed:20713166};
DE Includes:
DE RecName: Full=Dethiobiotin synthetase {ECO:0000303|PubMed:20713166};
DE Short=DTB synthetase {ECO:0000303|PubMed:20713166};
DE Short=DTBS {ECO:0000303|PubMed:20713166};
DE EC=6.3.3.3 {ECO:0000305|PubMed:20713166};
DE Includes:
DE RecName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000303|PubMed:20713166};
DE Short=DAPA AT {ECO:0000303|PubMed:20713166};
DE Short=DAPA aminotransferase {ECO:0000303|PubMed:20713166};
DE EC=2.6.1.62 {ECO:0000305|PubMed:20713166};
DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000250|UniProtKB:B0F481};
DE Short=DANS {ECO:0000250|UniProtKB:B0F481};
DE AltName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000250|UniProtKB:B0F481};
DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000250|UniProtKB:B0F481};
GN Name=bioDA {ECO:0000303|PubMed:20713166}; ORFNames=ANIA_06644;
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, MUTAGENESIS OF GLY-645, PATHWAY, AND BIOTECHNOLOGY.
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: Bifunctional enzyme; part of the cluster involved in the
CC biosynthesis of biotin (also known as vitamin B8 or vitamin H), a
CC 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 a mechanistically unusual reaction, the
CC ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of
CC 7,8-diaminopelargonic acid (DAPA) to form an ureido ring
CC (PubMed:20713166). Catalyzes also the transfer of the alpha-amino group
CC from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
CC (KAPA) to form 7,8-diaminopelargonic acid (DAPA) (PubMed:20713166). It
CC is the only animotransferase known to utilize SAM as an amino donor (By
CC similarity). {ECO:0000250|UniProtKB:B0F481,
CC ECO:0000269|PubMed:20713166}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC ChEBI:CHEBI:456216; EC=6.3.3.3;
CC Evidence={ECO:0000305|PubMed:20713166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine =
CC (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-
CC oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469;
CC EC=2.6.1.62; Evidence={ECO:0000305|PubMed:20713166};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B0F481};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:B0F481};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 1/2. {ECO:0000305|PubMed:20713166}.
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC {ECO:0000305|PubMed:20713166}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:B0F481}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:B0F481}.
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 -!- BIOTECHNOLOGY: Recovery of biotin-prototrophic clones from
CC transformation of biotin-auxotrophic mutants suggests that bioDA could
CC be usedas a new and convenient genetic marker for transformation.
CC {ECO:0000269|PubMed:20713166}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the dethiobiotin
CC synthetase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-III
CC pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001301; CBF71161.1; -; Genomic_DNA.
DR RefSeq; XP_664248.1; XM_659156.1.
DR AlphaFoldDB; Q5AYI6; -.
DR SMR; Q5AYI6; -.
DR STRING; 162425.CADANIAP00007426; -.
DR EnsemblFungi; CBF71161; CBF71161; ANIA_06644.
DR EnsemblFungi; EAA58173; EAA58173; AN6644.2.
DR GeneID; 2870397; -.
DR KEGG; ani:AN6644.2; -.
DR VEuPathDB; FungiDB:AN6644; -.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_010794_0_0_1; -.
DR InParanoid; Q5AYI6; -.
DR OMA; KGWASRA; -.
DR OrthoDB; 289012at2759; -.
DR UniPathway; UPA00078; UER00160.
DR UniPathway; UPA00078; UER00161.
DR Proteomes; UP000000560; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IMP:AspGD.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00336; BioD; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR004472; DTB_synth_BioD.
DR InterPro; IPR027417; P-loop_NTPase.
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; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; ATP-binding; Biotin biosynthesis; Ligase; Magnesium;
KW Metal-binding; Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transit peptide.
FT CHAIN 1..787
FT /note="Bifunctional dethiobiotin
FT synthetase/adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000449412"
FT BINDING 23..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 123..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 184..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P13000"
FT BINDING 323..324
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 384..385
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 421
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 582
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 611
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 645
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 646..647
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT BINDING 756
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250|UniProtKB:B0F481"
FT SITE 276
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT MUTAGEN 645
FT /note="G->R: In biA2; leads the requirement of either
FT biotin or dethiobiotin for growth."
FT /evidence="ECO:0000269|PubMed:20713166"
SQ SEQUENCE 787 AA; 86662 MW; 7CA2AB3977E4F3E9 CRC64;
MAPVGAALWR SLRAHQVYGA NTDVGKTIVS TFLCNAVNRL KNQGKSAFLK PVSTGPLDEA
DDRHLQRHAP NTLTKCLYQF DEPVSPHIAA KTFAIPRDDE ILSSVHRTLS DWANDGVGFA
LVETAGGVHS PGPNGNSQAD LYRPLRLPII LVADSRLGGI SSSISAYESL LLRGYDVHSV
LLFKDDYYQN HEYLGNYFRG KSIPLVPVPA PPRRPQEQDP DSRARDLEAL DKYYSSVTKS
TDVVSLLDEL VLKNKQRVEY LDEMASRAQK TIWYPFTQHH GMAAKDITPI DSAYDDFFQT
YVTADRSAQQ GRLQATFDGS ASWWTQGLGH GNPGLALSAA YAAGRYGHVM FPGNIHEPAL
ALAESLLKTV DNPRLQKVFY TDNGSTGMEV ALKMGLRAAC DRYGWDASKE QINILGLKGS
YHGDTIGVMD CSEPSTYNQR VEWYRGRGHW FDFPLVKMSQ GVWQVEVPAT LQASLGGNQQ
FSSLDAVFDV ESRVRSDAGQ RYRKYILETI ERLVTQEGKK FGALIMEPII LGAGGMLFCD
PLFQRCLADV VRGNPQLFNR GRLTEPQPQT DLSWSGLPVI FDEVFTGLYR LGRKSSASFL
GVNPDIAVNA KLLTGGLVPL CTTLASNEIF NAFTSPEKRD ALLHGHSYTA HAVGCQVALD
SLRTMNNMDE DGSWNDFKND WKQPHAGDTA RVWSVWSHKL LHNLSHAESV DGVFAIGSVL
SISLKDAEGA GYTSTAAKGL QTRLAAGGPQ FNVHSRVLGN VLYLMSSVTS KQETLRTIEG
ILREALL
