ID   BIOAB_BACT6             Reviewed;         744 AA.
AC   E6SRG2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
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=Bache_2094;
OS   Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG
OS   15421 / P 36-108).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=693979;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108;
RX   PubMed=21475586; DOI=10.4056/sigs.1513795;
RA   Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brambilla E.,
RA   Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT   "Complete genome sequence of Bacteroides helcogenes type strain (P 36-
RT   108).";
RL   Stand. Genomic Sci. 4:45-53(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002352; ADV44065.1; -; Genomic_DNA.
DR   RefSeq; WP_013547658.1; NC_014933.1.
DR   AlphaFoldDB; E6SRG2; -.
DR   SMR; E6SRG2; -.
DR   STRING; 693979.Bache_2094; -.
DR   KEGG; bhl:Bache_2094; -.
DR   PATRIC; fig|693979.3.peg.2204; -.
DR   eggNOG; COG0161; Bacteria.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_016922_9_1_10; -.
DR   OrthoDB; 9807885at2; -.
DR   UniPathway; UPA00078; UER00160.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000008630; 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; SFLDG01060; BATS_domain_containing; 1.
DR   SFLD; SFLDG01278; biotin_synthase_like; 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..744
FT                   /note="Biotin biosynthesis bifunctional protein BioAB"
FT                   /id="PRO_0000411134"
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         710
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   744 AA;  82983 MW;  6D94D64153D41FC0 CRC64;
     MTVNELKEQV LEGNFISREE AEWLAAQSDK EALYEAAHEI TRTLASEEFD MCSIINAKSG
     RCPENCKWCA QSSHYKTKAD VYDLVDKEEC LRHAKYNEEQ GVARFSLVTS GRKPSGKNME
     KLCEAARHMR RHSSIQLCAS LGLLNEEEML ALHDAGITRY HCNLETAPSY FSNLCSTHTQ
     AEKIRTLKAA RNAGMDICSG GIIGMGESME QRIEFAFTLK DMEVQSIPIN LLSPIPGTPL
     ERQEPLNEEE ILTTIALFRF INPRAFLRFA GGRSQLSTEA VRKALHIGIN SAIVGDLLTT
     IGSKVSEDKT LIEEAGYRFS DSQFDREHLW HPYTSTTDPL PVYKVEQAEG ATITLESGQT
     LIEGMSSWWC AIHGYNNPVL NHAATEQIGK MSHVMFGGLT HEPAIELGKL LLPLVPPSMQ
     KIFYADSGSV AVEVALKMAV QYWYGKGKEK KNNFVTIRSG YHGDTWNAMS VCDPVTGMHS
     LFGSSLPIRY FAPQPRSRYD GDWDAGDSME LQNIIEQHHE ELAALILEPI VQGAGGMWFY
     HPQYLREAAR LCKQYGLLLI FDEIATGFGR TGKLFAWEHA GTEPDIMCIG KALTGGYMTL
     SAVLTTNEVA DAISNHSPGV FMHGPTFMGN PLACAVACAS VRLLTSPVYD WQGKVNRISM
     QLREELAPAR QLPQVKDVRI LGAIGVIEVT ENVDMAWMQR RFVEEGIWVR PFGKLVYLMP
     PFIIEPEQLT KLTSGLIKII KEML
//