ID   BIOAB_BACFN             Reviewed;         748 AA.
AC   Q5LEY1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
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=BF1617;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC   Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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   -!- 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; CR626927; CAH07318.1; -; Genomic_DNA.
DR   RefSeq; WP_010992602.1; NZ_UFTH01000001.1.
DR   AlphaFoldDB; Q5LEY1; -.
DR   SMR; Q5LEY1; -.
DR   PaxDb; 272559-BF9343_1537; -.
DR   KEGG; bfs:BF9343_1537; -.
DR   eggNOG; COG0161; Bacteria.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_016922_9_1_10; -.
DR   UniPathway; UPA00078; UER00160.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000006731; 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   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR010722; BATS_dom.
DR   InterPro; IPR005815; BioA.
DR   InterPro; IPR002684; Biotin_synth/BioAB.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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   NCBIfam; TIGR00508; bioA; 1.
DR   NCBIfam; TIGR00433; bioB; 1.
DR   PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01278; biotin_synthase_like; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00876; BATS; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 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   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..748
FT                   /note="Biotin biosynthesis bifunctional protein BioAB"
FT                   /id="PRO_0000381227"
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;  83164 MW;  611586B40A861A51 CRC64;
     MTIEEIKNQV LQGTAISREQ AEWLALYPRK EELYDAAHDI TTACASQEFD MCSIINARSG
     RCPENCKWCA QSSHYKTKAD VYDLVSADEC 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 LEYLLEKHAD ELAAFILEPI VQGAGGMRFY
     HPEYLKEAAR LCHRYGVLLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL
     SAVLTTNEVA DCISNHAPGA FMHGPTFMGN PLACAVACAS VRLLLTSGWQ ENVKRIEAQL
     NRELAPAREL PQVADVRVLG AIGVIEMKEP VNMAYLQRRF VEEGIWLRPF GKLIYVMPPF
     IITPEQLTKL TEGMIRIISN GLPGSQTK
//