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8-amino-7-oxononanoate synthase (AONS) (EC 2.3.1.47) (7-keto-8-amino-pelargonic acid synthase) (7-KAP synthase) (KAPA synthase) (8-amino-7-ketopelargonate synthase) (Biotin synthase 4) (Biotin synthase F) (AtbioF)

 BIOF_ARATH              Reviewed;         476 AA.
Q8GW43; Q2QKD2; Q9LZ63;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
14-OCT-2015, sequence version 2.
30-AUG-2017, entry version 115.
RecName: Full=8-amino-7-oxononanoate synthase;
Short=AONS;
EC=2.3.1.47 {ECO:0000269|PubMed:16299174};
AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000303|PubMed:16299174};
Short=7-KAP synthase {ECO:0000303|PubMed:16299174};
Short=KAPA synthase {ECO:0000303|PubMed:16299174};
AltName: Full=8-amino-7-ketopelargonate synthase;
AltName: Full=Biotin synthase 4 {ECO:0000303|PubMed:22126457};
AltName: Full=Biotin synthase F {ECO:0000303|PubMed:16299174};
Short=AtbioF {ECO:0000303|PubMed:16299174};
Name=BIOF {ECO:0000303|PubMed:16299174};
Synonyms=BIO4 {ECO:0000303|PubMed:22126457};
OrderedLocusNames=At5g04620 {ECO:0000312|EMBL:AED90766.1};
ORFNames=T32M21.220 {ECO:0000312|EMBL:CAB85568.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:BAC43668.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, COFACTOR,
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND PATHWAY.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=16299174; DOI=10.1104/pp.105.070144;
Pinon V., Ravanel S., Douce R., Alban C.;
"Biotin synthesis in plants. The first committed step of the pathway
is catalyzed by a cytosolic 7-keto-8-aminopelargonic acid synthase.";
Plant Physiol. 139:1666-1676(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF Clones.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN PTS1, AND MUTAGENESIS OF
474-PRO--LEU-476.
STRAIN=cv. Columbia;
PubMed=21730067; DOI=10.1074/jbc.M111.247338;
Tanabe Y., Maruyama J., Yamaoka S., Yahagi D., Matsuo I., Tsutsumi N.,
Kitamoto K.;
"Peroxisomes are involved in biotin biosynthesis in Aspergillus and
Arabidopsis.";
J. Biol. Chem. 286:30455-30461(2011).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=22126457; DOI=10.1111/j.1365-313X.2011.04871.x;
Li J., Brader G., Helenius E., Kariola T., Palva E.T.;
"Biotin deficiency causes spontaneous cell death and activation of
defense signaling.";
Plant J. 70:315-326(2012).
-!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-
[acyl-carrier protein] and L-alanine to produce 8-amino-7-
oxononanoate (AON), [acyl-carrier protein], and carbon dioxide
(PubMed:16299174, PubMed:21730067). Required for the biosynthesis
of D-biotin that prevents light-mediated cell death and modulates
defense gene expression, probably by avoiding hydrogen peroxide
H(2)O(2) accumulation (PubMed:22126457).
{ECO:0000269|PubMed:16299174, ECO:0000269|PubMed:21730067,
ECO:0000269|PubMed:22126457}.
-!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] + L-alanine =
8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein].
{ECO:0000269|PubMed:16299174}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:16299174};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.6 uM for pimeloyl-CoA (at pH 7.5 and 30 degrees Celsius)
{ECO:0000269|PubMed:16299174};
KM=1.4 uM for L-alanine (at pH 7.5 and 30 degrees Celsius)
{ECO:0000269|PubMed:16299174};
Vmax=110 nmol/min/mg enzyme with pimeloyl-CoA as substrate (at
pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16299174};
Vmax=125 nmol/min/mg enzyme with L-alanine as substrate (at pH
7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:16299174};
Note=kcat is 0.1 sec(-1) with pimeloyl-CoA as substrate. kcat is
0.11 sec(-1) with L-alanine as substrate.
{ECO:0000269|PubMed:16299174};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 8-amino-7-
oxononanoate from pimeloyl-CoA: step 1/1.
{ECO:0000269|PubMed:16299174}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16299174}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:16299174}. Peroxisome
{ECO:0000269|PubMed:21730067}. Note=The cytosolic localization
observed in PubMed:16299174 is probably due to the lack of PTS1
domain at the C-terminus of the reporter gene construct.
{ECO:0000303|PubMed:21730067}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8GW43-1; Sequence=Displayed;
Name=2;
IsoId=Q8GW43-2; Sequence=VSP_057924;
Note=No experimental confirmation available.
{ECO:0000312|EMBL:AED90765.1};
-!- DOMAIN: The C-terminus PTS1 domain (474-476) is required for
biotin biosynthesis activity and peroxisomal subcellular
localization. {ECO:0000269|PubMed:21730067}.
-!- DISRUPTION PHENOTYPE: Light-dependent spontaneous cell death due
to the absence of D-biotin. Strong accumulation of hydrogen
peroxide H(2)O(2) and constitutive up-regulation of reactive
oxygen species- (ROS)-responsive and defense genes. Reduction of
both chloroplastic and nuclear biotinylated proteins. Accumulation
of conjugated salicylic acid (SA). {ECO:0000269|PubMed:22126457}.
-!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
aminotransferase family. BioF subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB85568.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ017966; AAY82238.1; -; mRNA.
EMBL; AL162875; CAB85568.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED90765.1; -; Genomic_DNA.
EMBL; CP002688; AED90766.1; -; Genomic_DNA.
EMBL; AK119095; BAC43668.1; -; mRNA.
EMBL; BT026507; ABH04614.1; -; mRNA.
PIR; T48458; T48458.
RefSeq; NP_196082.2; NM_120544.3. [Q8GW43-2]
RefSeq; NP_974731.1; NM_203002.4. [Q8GW43-1]
UniGene; At.46019; -.
ProteinModelPortal; Q8GW43; -.
SMR; Q8GW43; -.
STRING; 3702.AT5G04620.2; -.
PaxDb; Q8GW43; -.
EnsemblPlants; AT5G04620.1; AT5G04620.1; AT5G04620. [Q8GW43-2]
EnsemblPlants; AT5G04620.2; AT5G04620.2; AT5G04620. [Q8GW43-1]
GeneID; 830339; -.
Gramene; AT5G04620.1; AT5G04620.1; AT5G04620.
Gramene; AT5G04620.2; AT5G04620.2; AT5G04620.
KEGG; ath:AT5G04620; -.
Araport; AT5G04620; -.
TAIR; locus:2184397; AT5G04620.
eggNOG; KOG1359; Eukaryota.
eggNOG; COG0156; LUCA.
HOGENOM; HOG000221021; -.
KO; K00652; -.
OMA; FGTIGEN; -.
OrthoDB; EOG09360CK4; -.
PhylomeDB; Q8GW43; -.
BRENDA; 2.3.1.47; 399.
Reactome; R-ATH-189451; Heme biosynthesis.
UniPathway; UPA00078; UER00159.
PRO; PR:Q8GW43; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8GW43; baseline and differential.
Genevisible; Q8GW43; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009102; P:biotin biosynthetic process; IDA:TAIR.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
Alternative splicing; Biotin biosynthesis; Complete proteome;
Cytoplasm; Peroxisome; Pyridoxal phosphate; Reference proteome;
Transferase.
CHAIN 1 476 8-amino-7-oxononanoate synthase.
/FTId=PRO_0000434308.
REGION 171 172 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P12998}.
REGION 285 288 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P12998}.
REGION 316 319 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P12998}.
MOTIF 474 476 Peroxisomal targeting signal PTS1.
{ECO:0000269|PubMed:21730067}.
BINDING 24 24 Substrate.
{ECO:0000250|UniProtKB:P12998}.
BINDING 210 210 Substrate.
{ECO:0000250|UniProtKB:P12998}.
BINDING 260 260 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P12998}.
BINDING 427 427 Substrate.
{ECO:0000250|UniProtKB:P12998}.
MOD_RES 319 319 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P12998}.
VAR_SEQ 1 133 Missing (in isoform 2).
/FTId=VSP_057924.
MUTAGEN 474 476 Missing: Incorrect cytosolic localization
and loss of biotin synthase activity.
{ECO:0000269|PubMed:21730067}.
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


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