BIOAB_BACFR
ID BIOAB_BACFR Reviewed; 748 AA.
AC Q64VX4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=BF1603;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD48352.1; -; Genomic_DNA.
DR RefSeq; WP_011202495.1; NC_006347.1.
DR RefSeq; YP_098886.1; NC_006347.1.
DR AlphaFoldDB; Q64VX4; -.
DR SMR; Q64VX4; -.
DR STRING; 295405.BF1603; -.
DR PRIDE; Q64VX4; -.
DR EnsemblBacteria; BAD48352; BAD48352; BF1603.
DR KEGG; bfr:BF1603; -.
DR PATRIC; fig|295405.11.peg.1560; -.
DR HOGENOM; CLU_016922_9_1_10; -.
DR OMA; KWCAQSS; -.
DR UniPathway; UPA00078; UER00160.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000002197; 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_0000381228"
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 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; 83163 MW; EBEAA61DCA8BBD73 CRC64;
MTIEEIKNQV LQGTAISREQ AGWLALYPRK EELYDAAHDI TTACASQEFD MCSIINARSG
RCPENCKWCA QSSHYKTKAD VYDLVSAEEC LRQAKYNEAQ GVNRFSLVTS GRKPSPKNMK
ELCVAVRRMR RHSSIRLCAS LGLLDEEELQ ALYDAGVTRY HCNLETAPSH FDSLCTTHTQ
EQKLKTLYAA 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 LEHLLEKHAD ELAAFILEPI VQGAGGMRFY
HPEYLREAAR LCHRYGVLLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL
SAVLTTNEVA DCISNHAPGA FMHGPTFMGN PLACAVACAS VRLLLTSGWQ ENVKRIEAQL
NRELAPAREL PQVADVRVLG AIGVIEMKEP VNMAYLQRRF VEEGIWLRPF GKLIYVMPPF
IITPEQLTKL TEGMIRIISN GLPGSQTK
