BIOAB_BACTN
ID BIOAB_BACTN Reviewed; 741 AA.
AC Q8A7T2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=BT_1442;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAO76549.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE015928; AAO76549.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_810355.1; NC_004663.1.
DR AlphaFoldDB; Q8A7T2; -.
DR SMR; Q8A7T2; -.
DR STRING; 226186.BT_1442; -.
DR PaxDb; Q8A7T2; -.
DR PRIDE; Q8A7T2; -.
DR EnsemblBacteria; AAO76549; AAO76549; BT_1442.
DR KEGG; bth:BT_1442; -.
DR PATRIC; fig|226186.12.peg.1474; -.
DR eggNOG; COG0161; Bacteria.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_016922_9_0_10; -.
DR InParanoid; Q8A7T2; -.
DR OMA; KWCAQSS; -.
DR UniPathway; UPA00078; UER00160.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000001414; 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; IBA:GO_Central.
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; IBA:GO_Central.
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 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 Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..741
FT /note="Biotin biosynthesis bifunctional protein BioAB"
FT /id="PRO_0000381234"
FT DOMAIN 44..273
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 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
