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P50277 (BIOA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

EC=2.6.1.62
Alternative name(s):
7,8-diamino-pelargonic acid aminotransferase
Short name=DAPA AT
Short name=DAPA aminotransferase
Diaminopelargonic acid synthase
Gene names
Name:BIO3
Ordered Locus Names:YNR058W
ORF Names:N3510
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. Ref.1

Catalytic activity

S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MSH3P253361EBI-3632,EBI-11362

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
PRO_0000120378

Regions

Region65 – 6627-keto-8-aminopelargonic acid binding By similarity
Region126 – 1272Pyridoxal phosphate binding By similarity

Sites

Binding site2617-keto-8-aminopelargonic acid By similarity
Binding site2701Pyridoxal phosphate By similarity
Binding site31417-keto-8-aminopelargonic acid By similarity
Binding site35017-keto-8-aminopelargonic acid; via carbonyl oxygen By similarity
Binding site3521Pyridoxal phosphate By similarity
Binding site44117-keto-8-aminopelargonic acid By similarity

Amino acid modifications

Modified residue3141N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant2291K → E in strain: ATCC 28383 and ATCC 204626. Ref.2
Natural variant2951H → R in strain: ATCC 28383 and ATCC 204626. Ref.2
Natural variant3841N → D in strain: ATCC 28383 and ATCC 204626. Ref.2

Experimental info

Sequence conflict1401S → P in AAU09779. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P50277 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 00A8BC42DCBED19A

FASTA48053,709
        10         20         30         40         50         60 
MSQEISYTPD VAELLDFDKK HIWHPYTSLS SPLNVYPVKS AHGCKLVLDT DSPVDVEVID 

        70         80         90        100        110        120 
AMSSWWCVIH GYNNPELNEA LTKQMLKFSH VLLGGFTHKG AVNLVQKLLK VIDEPSLQYC 

       130        140        150        160        170        180 
FLADSGSVAV EVALKMALQS NMSGEATKNR TKFLTIKNGY HGDTFGAMSV CDPENSMHHI 

       190        200        210        220        230        240 
YNDRLSENIF AQAPSIVDGL PTSQNGFEDH WNAEEVTDLK KQFELHSDKI CAVILEPILQ 

       250        260        270        280        290        300 
GAGGLRPYHP QFLIEVQKLC NQYDVLFIMD EIATGFGRTG EIFAFKHCQK YQDQHGISPS 

       310        320        330        340        350        360 
DQIKVVPDIL CVGKGLTSGY MTMSAVVVND KVASRISSPN SPTGGCFMHG PTFMGNALAC 

       370        380        390        400        410        420 
SVAEKSMDIL LRGEWRKQVS AIENQIYREL YQYIKNPDNG LIGTVVKRVS VIGAVGIVEL 

       430        440        450        460        470        480 
YKKTDPEWFQ KKFISKGVHI RPFNCLCYIM PPYVITTEEL TKVNQVLIEV LHEWKSHINQ 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the biotin biosynthesis pathway in Saccharomyces cerevisiae and evidence for a cluster containing BIO5, a novel gene involved in vitamer uptake."
Phalip V., Kuhn I., Lemoine Y., Jeltsch J.-M.
Gene 232:43-51(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]"Identification and characterization of a novel biotin biosynthesis gene in Saccharomyces cerevisiae."
Wu H., Ito K., Shimoi H.
Appl. Environ. Microbiol. 71:6845-6855(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-229; ARG-295 AND ASP-384.
Strain: ATCC 204626 / S288c / A364A.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U47112 Genomic DNA. Translation: AAA88905.1.
U53467 Genomic DNA. Translation: AAB63970.1.
AB200248 Genomic DNA. Translation: BAE00005.1.
Z71673 Genomic DNA. Translation: CAA96340.1.
AY723862 Genomic DNA. Translation: AAU09779.1.
BK006947 Genomic DNA. Translation: DAA10599.1.
PIRS63390.
RefSeqNP_014456.1. NM_001183235.1.

3D structure databases

ProteinModelPortalP50277.
SMRP50277. Positions 15-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35884. 9 interactions.
DIPDIP-4822N.
IntActP50277. 1 interaction.
MINTMINT-562496.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNR058W; YNR058W; YNR058W.
GeneID855795.
KEGGsce:YNR058W.

Organism-specific databases

CYGDYNR058w.
SGDS000005341. BIO3.

Phylogenomic databases

eggNOGCOG0161.
HOGENOMHOG000020209.
KOK00833.
OMAMATMAIC.
OrthoDBEOG7Q2NFK.

Enzyme and pathway databases

BioCycYEAST:YNR058W-MONOMER.
UniPathwayUPA00078; UER00160.

Gene expression databases

GenevestigatorP50277.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00508. bioA. 1 hit.
ProtoNetSearch...

Other

NextBio980291.
PROP50277.

Entry information

Entry nameBIOA_YEAST
AccessionPrimary (citable) accession number: P50277
Secondary accession number(s): D6W1N3, E9P967, Q4R1J0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways