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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_BACTN             Reviewed;         741 AA.
Q8A7T2;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 2.
05-JUL-2017, entry version 104.
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=BT_1442;
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
10582 / E50 / VPI-5482).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
Bacteroides.
NCBI_TaxID=226186;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
PubMed=12663928; DOI=10.1126/science.1080029;
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAO76549.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AE015928; AAO76549.1; ALT_INIT; Genomic_DNA.
RefSeq; NP_810355.1; NC_004663.1.
RefSeq; WP_011107782.1; NC_004663.1.
ProteinModelPortal; Q8A7T2; -.
SMR; Q8A7T2; -.
STRING; 226186.BT_1442; -.
PaxDb; Q8A7T2; -.
EnsemblBacteria; AAO76549; AAO76549; BT_1442.
GeneID; 1076134; -.
KEGG; bth:BT_1442; -.
PATRIC; fig|226186.12.peg.1474; -.
eggNOG; ENOG4105C8Y; Bacteria.
eggNOG; COG0161; LUCA.
eggNOG; COG0502; LUCA.
HOGENOM; HOG000138865; -.
InParanoid; Q8A7T2; -.
KO; K00833; -.
OMA; KWCAQSS; -.
OrthoDB; POG091H01IB; -.
UniPathway; UPA00078; UER00160.
UniPathway; UPA00078; UER00162.
Proteomes; UP000001414; 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; IPR005815; BioA.
InterPro; IPR002684; Biotin_synth/BioAB.
InterPro; IPR006638; Elp3/MiaB/NifB.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
InterPro; IPR007197; rSAM.
Pfam; PF00202; Aminotran_3; 1.
Pfam; PF06968; BATS; 1.
Pfam; PF04055; Radical_SAM; 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; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 741 Biotin biosynthesis bifunctional protein
BioAB.
/FTId=PRO_0000381234.
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 741 AA; 82116 MW; 6FA1F6EE5879C1DD CRC64;
MTLQEIKDQV LAGFDISSAQ ATWLANMADS EALYAAAHEI TITCASHEFD MCSIINAKSG
RCPENCKWCA QSSHYKTQAE IYDLLPAEEC LRQAKYNESQ DVNRFSLVTS GRKPSPKQIS
QLCDAARLMR KHSSIQLCAS LGLLNEEELR ALHTAGITRY HCNLETAPSY FPTLCSTHTQ
EQKLATLDAA RRVGMDICCG GIIGMGETME QRIEFAFTLA ELNVQSIPIN LLSPIPGTPL
ENEKALSEEE ILRTIALFRF INPTAFLRFA GGRSQLTPEA MRKALFVGIN SAIVGDLLTT
LGSKVSDDKK MILEEGYHFA DSQFDREHLW HPYTSTTDPL PVYKVKRADG ATITLEDGRT
LIEGMSSWWC AVHGYNHPVL NQAAKDQLDK MSHVMFGGLT HDPAIELGKL LLPLVPPSMQ
KIFYADSGSV AVEVALKMAV QYWYAAGKPD KNNFVTIRSG YHGDTWNAMS VCDPVTGMHS
LFGSSLPVRY FVPAPSSRFD GEWNPDEIIP LRETIEKHSK ELAALILEPI VQGAGGMWFY
HPQYLREAEK LCKEHDILLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL
SAVLASNQIA DTISNHAPKA FMHGPTFMGN PLACAVACAS VRLLLDSGWA ENVKRIEAQL
KEELAPARKF PQVADVRILG AIGVIQTERS VSMAYMQRRF VEEGIWVRPF GKLVYLMPPF
IISPEQLSKL TSGVLKIVRE M


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