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Biotin biosynthesis bifunctional protein BioAB [Includes: Biotin synthase BioB (EC 2.8.1.6); Adenosylmethionine-8-amino-7-oxononanoate aminotransferase BioA (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)]

 BIOAB_BACFR             Reviewed;         748 AA.
Q64VX4;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 1.
23-MAY-2018, entry version 85.
RecName: Full=Biotin biosynthesis bifunctional protein BioAB;
Includes:
RecName: Full=Biotin synthase BioB;
EC=2.8.1.6;
Includes:
RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase BioA;
EC=2.6.1.62;
AltName: Full=7,8-diamino-pelargonic acid aminotransferase;
Short=DAPA AT;
Short=DAPA aminotransferase;
AltName: Full=7,8-diaminononanoate synthase;
Short=DANS;
AltName: Full=Diaminopelargonic acid synthase;
Name=bioB; OrderedLocusNames=BF1603;
Bacteroides fragilis (strain YCH46).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
Bacteroides.
NCBI_TaxID=295405;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
PubMed=15466707; DOI=10.1073/pnas.0404172101;
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA
inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
-!- FUNCTION: Catalyzes two activities which are involved in the
biotine biosynthesis: the conversion of dethiobiotin (DTB) to
biotin by the insertion of a sulfur atom into dethiobiotin via a
radical-based mechanism, and the transfer of the alpha-amino group
from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic
acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S-
adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin +
(sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2
oxidized [2Fe-2S] ferredoxin.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
diaminononanoate.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
cysteines and an exchangeable S-adenosyl-L-methionine.
{ECO:0000250};
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
cysteines and 1 arginine. {ECO:0000250};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 2/2.
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
superfamily. Biotin synthase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class-III
pyridoxal-phosphate-dependent aminotransferase family. BioA
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AP006841; BAD48352.1; -; Genomic_DNA.
RefSeq; WP_011202495.1; NC_006347.1.
RefSeq; YP_098886.1; NC_006347.1.
ProteinModelPortal; Q64VX4; -.
SMR; Q64VX4; -.
PRIDE; Q64VX4; -.
EnsemblBacteria; BAD48352; BAD48352; BF1603.
GeneID; 3082802; -.
KEGG; bfr:BF1603; -.
PATRIC; fig|295405.11.peg.1560; -.
HOGENOM; HOG000032982; -.
KO; K00833; -.
OMA; KWCAQSS; -.
OrthoDB; POG091H01IB; -.
UniPathway; UPA00078; UER00160.
UniPathway; UPA00078; UER00162.
Proteomes; UP000002197; Chromosome.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_00834; BioA; 1.
HAMAP; MF_01694; BioB; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR010722; BATS_dom.
InterPro; IPR034416; BATS_domain_containing.
InterPro; IPR005815; BioA.
InterPro; IPR002684; Biotin_synth/BioAB.
InterPro; IPR006638; Elp3/MiaB/NifB.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
InterPro; IPR007197; rSAM.
Pfam; PF00202; Aminotran_3; 1.
Pfam; PF06968; BATS; 1.
Pfam; PF04055; Radical_SAM; 1.
SFLD; SFLDG01060; BATS_domain_containing; 1.
SFLD; SFLDG01278; biotin_synthase_like; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
SMART; SM00876; BATS; 1.
SMART; SM00729; Elp3; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00508; bioA; 1.
TIGRFAMs; TIGR00433; bioB; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
3: Inferred from homology;
2Fe-2S; 4Fe-4S; Aminotransferase; Biotin biosynthesis;
Complete proteome; Iron; Iron-sulfur; Metal-binding;
Multifunctional enzyme; Pyridoxal phosphate; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 748 Biotin biosynthesis bifunctional protein
BioAB.
/FTId=PRO_0000381228.
REGION 428 429 Pyridoxal phosphate binding.
REGION 625 626 Pyridoxal phosphate binding.
{ECO:0000250}.
METAL 62 62 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000250}.
METAL 66 66 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000250}.
METAL 69 69 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000250}.
METAL 106 106 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
METAL 138 138 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
METAL 198 198 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
METAL 268 268 Iron-sulfur 2 (2Fe-2S). {ECO:0000250}.
BINDING 368 368 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 461 461 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 562 562 Pyridoxal phosphate. {ECO:0000250}.
BINDING 591 591 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 624 624 7-keto-8-aminopelargonic acid; via
carbonyl oxygen. {ECO:0000250}.
BINDING 708 708 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
SITE 333 333 Participates in the substrate recognition
with KAPA and in a stacking interaction
with the adenine ring of SAM.
{ECO:0000250}.
MOD_RES 591 591 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
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


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