BIOF_ARATH
ID BIOF_ARATH Reviewed; 476 AA.
AC Q8GW43; Q2QKD2; Q9LZ63;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=8-amino-7-oxononanoate synthase;
DE Short=AONS;
DE EC=2.3.1.47 {ECO:0000269|PubMed:16299174};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000303|PubMed:16299174};
DE Short=7-KAP synthase {ECO:0000303|PubMed:16299174};
DE Short=KAPA synthase {ECO:0000303|PubMed:16299174};
DE AltName: Full=8-amino-7-ketopelargonate synthase;
DE AltName: Full=Biotin synthase 4 {ECO:0000303|PubMed:22126457};
DE AltName: Full=Biotin synthase F {ECO:0000303|PubMed:16299174};
DE Short=AtbioF {ECO:0000303|PubMed:16299174};
GN Name=BIOF {ECO:0000303|PubMed:16299174};
GN Synonyms=BIO4 {ECO:0000303|PubMed:22126457};
GN OrderedLocusNames=At5g04620 {ECO:0000312|EMBL:AED90766.1};
GN ORFNames=T32M21.220 {ECO:0000312|EMBL:CAB85568.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:BAC43668.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, COFACTOR,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND PATHWAY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=16299174; DOI=10.1104/pp.105.070144;
RA Pinon V., Ravanel S., Douce R., Alban C.;
RT "Biotin synthesis in plants. The first committed step of the pathway is
RT catalyzed by a cytosolic 7-keto-8-aminopelargonic acid synthase.";
RL Plant Physiol. 139:1666-1676(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN PTS1, AND MUTAGENESIS OF
RP 474-PRO--LEU-476.
RC STRAIN=cv. Columbia;
RX PubMed=21730067; DOI=10.1074/jbc.m111.247338;
RA Tanabe Y., Maruyama J., Yamaoka S., Yahagi D., Matsuo I., Tsutsumi N.,
RA Kitamoto K.;
RT "Peroxisomes are involved in biotin biosynthesis in Aspergillus and
RT Arabidopsis.";
RL J. Biol. Chem. 286:30455-30461(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22126457; DOI=10.1111/j.1365-313x.2011.04871.x;
RA Li J., Brader G., Helenius E., Kariola T., Palva E.T.;
RT "Biotin deficiency causes spontaneous cell death and activation of defense
RT signaling.";
RL Plant J. 70:315-326(2012).
CC -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-
CC carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC [acyl-carrier protein], and carbon dioxide (PubMed:16299174,
CC PubMed:21730067). Required for the biosynthesis of D-biotin that
CC prevents light-mediated cell death and modulates defense gene
CC expression, probably by avoiding hydrogen peroxide H(2)O(2)
CC accumulation (PubMed:22126457). {ECO:0000269|PubMed:16299174,
CC ECO:0000269|PubMed:21730067, ECO:0000269|PubMed:22126457}.
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:0000269|PubMed:16299174};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:16299174};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for pimeloyl-CoA (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16299174};
CC KM=1.4 uM for L-alanine (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16299174};
CC Vmax=110 nmol/min/mg enzyme with pimeloyl-CoA as substrate (at pH 7.5
CC and 30 degrees Celsius) {ECO:0000269|PubMed:16299174};
CC Vmax=125 nmol/min/mg enzyme with L-alanine as substrate (at pH 7.5
CC and 30 degrees Celsius) {ECO:0000269|PubMed:16299174};
CC Note=kcat is 0.1 sec(-1) with pimeloyl-CoA as substrate. kcat is 0.11
CC sec(-1) with L-alanine as substrate. {ECO:0000269|PubMed:16299174};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 8-amino-7-
CC oxononanoate from pimeloyl-CoA: step 1/1.
CC {ECO:0000269|PubMed:16299174}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16299174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16299174}.
CC Peroxisome {ECO:0000269|PubMed:21730067}. Note=The cytosolic
CC localization observed in PubMed:16299174 is probably due to the lack of
CC PTS1 domain at the C-terminus of the reporter gene construct.
CC {ECO:0000303|PubMed:21730067}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GW43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GW43-2; Sequence=VSP_057924;
CC -!- DOMAIN: The C-terminus PTS1 domain (474-476) is required for biotin
CC biosynthesis activity and peroxisomal subcellular localization.
CC {ECO:0000269|PubMed:21730067}.
CC -!- DISRUPTION PHENOTYPE: Light-dependent spontaneous cell death due to the
CC absence of D-biotin. Strong accumulation of hydrogen peroxide H(2)O(2)
CC and constitutive up-regulation of reactive oxygen species- (ROS)-
CC responsive and defense genes. Reduction of both chloroplastic and
CC nuclear biotinylated proteins. Accumulation of conjugated salicylic
CC acid (SA). {ECO:0000269|PubMed:22126457}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB85568.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ017966; AAY82238.1; -; mRNA.
DR EMBL; AL162875; CAB85568.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90765.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90766.1; -; Genomic_DNA.
DR EMBL; AK119095; BAC43668.1; -; mRNA.
DR EMBL; BT026507; ABH04614.1; -; mRNA.
DR PIR; T48458; T48458.
DR RefSeq; NP_196082.2; NM_120544.3. [Q8GW43-2]
DR RefSeq; NP_974731.1; NM_203002.4. [Q8GW43-1]
DR AlphaFoldDB; Q8GW43; -.
DR SMR; Q8GW43; -.
DR STRING; 3702.AT5G04620.2; -.
DR PaxDb; Q8GW43; -.
DR PRIDE; Q8GW43; -.
DR ProteomicsDB; 240352; -. [Q8GW43-1]
DR EnsemblPlants; AT5G04620.1; AT5G04620.1; AT5G04620. [Q8GW43-2]
DR EnsemblPlants; AT5G04620.2; AT5G04620.2; AT5G04620. [Q8GW43-1]
DR GeneID; 830339; -.
DR Gramene; AT5G04620.1; AT5G04620.1; AT5G04620. [Q8GW43-2]
DR Gramene; AT5G04620.2; AT5G04620.2; AT5G04620. [Q8GW43-1]
DR KEGG; ath:AT5G04620; -.
DR Araport; AT5G04620; -.
DR TAIR; locus:2184397; AT5G04620.
DR eggNOG; KOG1359; Eukaryota.
DR HOGENOM; CLU_015846_11_2_1; -.
DR OMA; MDTHGFG; -.
DR PhylomeDB; Q8GW43; -.
DR BRENDA; 2.3.1.47; 399.
DR UniPathway; UPA00078; UER00159.
DR PRO; PR:Q8GW43; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GW43; baseline and differential.
DR Genevisible; Q8GW43; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
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; IDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Biotin biosynthesis; Cytoplasm; Peroxisome;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..476
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000434308"
FT MOTIF 474..476
FT /note="Peroxisomal targeting signal PTS1"
FT /evidence="ECO:0000269|PubMed:21730067"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 171..172
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 260
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 285..288
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 316..319
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12998"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 2)"
FT /id="VSP_057924"
FT MUTAGEN 474..476
FT /note="Missing: Incorrect cytosolic localization and loss
FT of biotin synthase activity."
FT /evidence="ECO:0000269|PubMed:21730067"
SQ SEQUENCE 476 AA; 52171 MW; F569F3675E6EC48C CRC64;
MADHSWDKTV EEAVNVLESR QILRSLRPIC MSRQNEEEIV KSRANGGDGY EVFDGLCQWD
RTSVEVSVSI PTFQKWLHDE PSNGEEIFSG DALAECRKGR FKKLLLFSGN DYLGLSSHPT
ISNAAANAVK EYGMGPKGSA LICGYTTYHR LLESSLAQLK KKEDCLVCPT GFAANMAAMV
AIGSVASLLA ASGKPLKNEK VAIFSDALNH ASIIDGVRLA ERQGNVEVFV YRHCDMYHLN
SLLSNCKMKR KVVVTDSLFS MDGDFAPMEE LSQLRKKYGF LLVIDDAHGT FVCGENGGGV
AEEFNCEADV DLCVGTLSKA AGCHGGFIAC SKKWKQLIQS RGRSFIFSTA IPVPMAAAAY
AAVVVARKEI WRRKAIWERV KEFKELSGVD ISSPIISLVV GNQEKALKAS RYLLKSGFHV
MAIRPPTVPP NSCRLRVTLS AAHTTEDVKK LITALSSCLD FDNTATHIPS FLFPKL
