BIOAB_BACF6
ID BIOAB_BACF6 Reviewed; 748 AA.
AC E1WTS4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Biotin biosynthesis bifunctional protein BioAB;
DE Includes:
DE RecName: Full=Biotin synthase BioB;
DE EC=2.8.1.6;
DE Includes:
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase BioA;
DE EC=2.6.1.62;
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase;
DE Short=DAPA AT;
DE Short=DAPA aminotransferase;
DE AltName: Full=7,8-diaminononanoate synthase;
DE Short=DANS;
DE AltName: Full=Diaminopelargonic acid synthase;
GN Name=bioB; OrderedLocusNames=BF638R_1618;
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R;
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(2010).
CC -!- FUNCTION: Catalyzes two activities which are involved in the biotine
CC biosynthesis: the conversion of dethiobiotin (DTB) to biotin by the
CC insertion of a sulfur atom into dethiobiotin via a radical-based
CC mechanism, and the transfer of the alpha-amino group from S-adenosyl-L-
CC methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-
CC diaminopelargonic acid (DAPA). {ECO:0000250}.
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 -!- 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;
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 2/2.
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. Biotin synthase 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}.
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DR EMBL; FQ312004; CBW22147.1; -; Genomic_DNA.
DR RefSeq; WP_009291978.1; NC_016776.1.
DR AlphaFoldDB; E1WTS4; -.
DR SMR; E1WTS4; -.
DR PRIDE; E1WTS4; -.
DR EnsemblBacteria; CBW22147; CBW22147; BF638R_1618.
DR KEGG; bfg:BF638R_1618; -.
DR PATRIC; fig|862962.3.peg.1624; -.
DR HOGENOM; CLU_016922_9_1_10; -.
DR OMA; KWCAQSS; -.
DR UniPathway; UPA00078; UER00160.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000008560; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00834; BioA; 1.
DR HAMAP; MF_01694; BioB; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR002684; Biotin_synth/BioAB.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR TIGRFAMs; TIGR00433; bioB; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; 4Fe-4S; Aminotransferase; Biotin biosynthesis; Iron; Iron-sulfur;
KW Metal-binding; Multifunctional enzyme; Pyridoxal phosphate;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..748
FT /note="Biotin biosynthesis bifunctional protein BioAB"
FT /id="PRO_0000411133"
FT DOMAIN 44..270
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250"
FT BINDING 428..429
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250"
FT BINDING 562
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 591
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250"
FT BINDING 625..626
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="(8S)-8-amino-7-oxononanoate"
FT /ligand_id="ChEBI:CHEBI:149468"
FT /evidence="ECO:0000250"
FT SITE 333
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"
FT MOD_RES 591
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 748 AA; 83211 MW; 12363C6F57D0DC52 CRC64;
MTIEEIKNQV LQGTAISREQ AEWLALYPRK EELYDAAHDI TTACASQEFD MCSIINARSG
RCPENCKWCA QSSHYKTKAD VYDLVSAEEC LRQAKYNEAQ GVNRFSLVTS GRKPSPKNMK
ELCVAARRMR RHSSIRLCAS LGLLDEEELQ ALYDAGVTRY HCNLETAPSH FDSLCTTHTQ
EQKLKTLHAA RRVGMDLCCG GIIGMGETVE QRIEFAFTLR DLNIQSIPIN LLQPIPGTPL
EHQSPLSEEE ILTTVALFRF INPAAYLRFA GGRSQLTPEA VRKSLYIGIN SAIVGDLLTT
LGSKVSDDKE MILSEGYHFA DSQFDREHLW HPYTSTSNPL PVYKVKRADG ATITLESGQT
LIEGMSSWWC AVHGYNHPIL NQAVQDQLSR MSHVMFGGLT HDPAIELGKL LLPLVPPSMQ
KIFYADSGSV AVEVALKMAV QYWYAAGKPE KNNFVTIRNG YHGDTWNAMS VCDPVTGMHS
IFGSALPIRH FLPAPSSRFG DEWNPEDIRP LEHLLEKHTD ELAAFILEPI VQGAGGMRFY
HPEYLREAAR LCHRYGVLLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL
SAVLTTNEVA DCISNHAPGA FMHGPTFMGN PLACAVACAS VRLLLTSGWQ ENVKRIEAQL
NRELAPAREL PQVADVRVLG AIGVIEMKEP VNMAYLQRRF VEEGIWLRPF GKLIYVMPPF
IITPEQLTKL TEGMIRIISN GLPGSQTK
