BIOB_ARATH
ID BIOB_ARATH Reviewed; 378 AA.
AC P54967;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Biotin synthase, mitochondrial;
DE EC=2.8.1.6;
DE Flags: Precursor;
GN Name=BIO2; Synonyms=BIOB; OrderedLocusNames=At2g43360; ORFNames=T01O24.10;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8819873; DOI=10.1104/pp.110.3.1021;
RA Weaver L.M., Yu F., Wurtele E.S., Nikolau B.J.;
RT "Characterization of the cDNA and gene coding for the biotin synthase of
RT Arabidopsis thaliana.";
RL Plant Physiol. 110:1021-1028(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8819333; DOI=10.1104/pp.112.1.371;
RA Patton D.A., Johnson M., Ward E.R.;
RT "Biotin synthase from Arabidopsis thaliana. cDNA isolation and
RT characterization of gene expression.";
RL Plant Physiol. 112:371-378(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8680961;
RA Baldet P., Ruffet M.L.;
RT "Biotin synthesis in higher plants: isolation of a cDNA encoding
RT Arabidopsis thaliana bioB-gene product equivalent by functional
RT complementation of a biotin auxotroph mutant bioB105 of Escherichia coli
RT K12.";
RL C. R. Acad. Sci. III, Sci. Vie 319:99-106(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP TYR-26.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-
CC 2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine +
CC [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:149473; EC=2.8.1.6;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC cysteines and 1 arginine. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25732537}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC family. {ECO:0000305}.
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DR EMBL; U24147; AAA80226.1; -; Genomic_DNA.
DR EMBL; U31806; AAC49445.1; -; mRNA.
DR EMBL; L34413; AAB39953.1; -; mRNA.
DR EMBL; AC002335; AAB64312.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10256.1; -; Genomic_DNA.
DR PIR; S71201; S71201.
DR RefSeq; NP_181864.1; NM_129897.4.
DR AlphaFoldDB; P54967; -.
DR SMR; P54967; -.
DR BioGRID; 4274; 1.
DR STRING; 3702.AT2G43360.1; -.
DR iPTMnet; P54967; -.
DR MetOSite; P54967; -.
DR PaxDb; P54967; -.
DR PRIDE; P54967; -.
DR ProteomicsDB; 240695; -.
DR EnsemblPlants; AT2G43360.1; AT2G43360.1; AT2G43360.
DR GeneID; 818937; -.
DR Gramene; AT2G43360.1; AT2G43360.1; AT2G43360.
DR KEGG; ath:AT2G43360; -.
DR Araport; AT2G43360; -.
DR TAIR; locus:2005497; AT2G43360.
DR eggNOG; KOG2900; Eukaryota.
DR HOGENOM; CLU_033172_1_2_1; -.
DR InParanoid; P54967; -.
DR OMA; ADRFCMG; -.
DR OrthoDB; 847045at2759; -.
DR PhylomeDB; P54967; -.
DR UniPathway; UPA00078; UER00162.
DR PRO; PR:P54967; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P54967; baseline and differential.
DR Genevisible; P54967; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004076; F:biotin synthase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01694; BioB; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR002684; Biotin_synth/BioAB.
DR InterPro; IPR024177; Biotin_synthase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR22976; PTHR22976; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF001619; Biotin_synth; 1.
DR SFLD; SFLDF00272; biotin_synthase; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00433; bioB; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Biotin biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 27..378
FT /note="Biotin synthase, mitochondrial"
FT /id="PRO_0000185565"
FT DOMAIN 79..308
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 357..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 41682 MW; B102E477E7353762 CRC64;
MMLVRSVFRS QLRPSVSGGL QSASCYSSLS AASAEAERTI REGPRNDWSR DEIKSVYDSP
LLDLLFHGAQ VHRHVHNFRE VQQCTLLSIK TGGCSEDCSY CPQSSRYSTG VKAQRLMSKD
AVIDAAKKAK EAGSTRFCMG AAWRDTIGRK TNFSQILEYI KEIRGMGMEV CCTLGMIEKQ
QALELKKAGL TAYNHNLDTS REYYPNVITT RSYDDRLETL SHVRDAGINV CSGGIIGLGE
AEEDRIGLLH TLATLPSHPE SVPINALLAV KGTPLEDQKP VEIWEMIRMI GTARIVMPKA
MVRLSAGRVR FSMSEQALCF LAGANSIFTG EKLLTTPNND FDADQLMFKT LGLIPKPPSF
SEDDSESENC EKVASASH
