ID   A0A4Q0U2X9_9BACE        Unreviewed;       745 AA.
AC   A0A4Q0U2X9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   12-OCT-2022, entry version 15.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00834, ECO:0000256|HAMAP-Rule:MF_01694};
DE   Includes:
DE     RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE              EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
DE     AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE     AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
DE     AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
DE              Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834};
DE              Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834};
DE              Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE   Includes:
DE     RecName: Full=Biotin synthase {ECO:0000256|HAMAP-Rule:MF_01694};
DE              EC=2.8.1.6 {ECO:0000256|HAMAP-Rule:MF_01694};
GN   Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
GN   Synonyms=bioB {ECO:0000256|HAMAP-Rule:MF_01694};
GN   ORFNames=DBK98_012355 {ECO:0000313|EMBL:QLK82887.1};
OS   Bacteroides sp. PHL 2737.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides; unclassified Bacteroides.
OX   NCBI_TaxID=2162637 {ECO:0000313|EMBL:QLK82887.1, ECO:0000313|Proteomes:UP000289538};
RN   [1] {ECO:0000313|EMBL:QLK82887.1, ECO:0000313|Proteomes:UP000289538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHL 2737 {ECO:0000313|EMBL:QLK82887.1,
RC   ECO:0000313|Proteomes:UP000289538};
RA   Eshaghi A., Graham C., Zitterman S.I., Kus J.V., Soares D., Patel S.N.;
RT   "Molecular Characterization of a multi-drug resistant invasive Bacteroides
RT   spp. isolate.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by
CC       the insertion of a sulfur atom into dethiobiotin via a radical-based
CC       mechanism. {ECO:0000256|HAMAP-Rule:MF_01694}.
CC   -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC       adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to
CC       form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase
CC       known to utilize SAM as an amino donor. {ECO:0000256|HAMAP-
CC       Rule:MF_00834}.
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:0000256|ARBA:ARBA00003991}.
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         Evidence={ECO:0000256|ARBA:ARBA00023417, ECO:0000256|HAMAP-
CC         Rule:MF_01694};
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; Evidence={ECO:0000256|ARBA:ARBA00033988,
CC         ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01694};
CC       Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC       cysteines and 1 arginine. {ECO:0000256|HAMAP-Rule:MF_01694};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01694};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01694};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005063, ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC       diaminononanoate: step 2/2. {ECO:0000256|ARBA:ARBA00004942,
CC       ECO:0000256|HAMAP-Rule:MF_01694}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01694}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00834}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01694}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-III
CC       pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
CC       {ECO:0000256|ARBA:ARBA00006507}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC       superfamily. Biotin synthase family. {ECO:0000256|ARBA:ARBA00005255}.
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; CP040630; QLK82887.1; -; Genomic_DNA.
DR   RefSeq; WP_005809132.1; NZ_CP040630.1.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000289538; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_01694};
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01694};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00834};
KW   Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW   Rule:MF_01694}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01694};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01694};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01694}; Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00834};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01694}; Transferase {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   DOMAIN          44..270
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01694"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01694"
FT   BINDING         69
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01694"
FT   BINDING         106
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01694"
FT   BINDING         138
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01694"
FT   BINDING         198
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01694"
FT   BINDING         268
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01694"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         428..429
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         562
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         591
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         624
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         625..626
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT   BINDING         708
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
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:0000256|HAMAP-Rule:MF_00834"
FT   MOD_RES         591
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
SQ   SEQUENCE   745 AA;  82990 MW;  4088131C528ECAEF CRC64;
     MTIEEIKNQV LQGTAISREQ AEWLAQFPRK EELYDAAHEI TRFCASQEFD MCSIINARSG
     RCPENCKWCA QSSHYKTKAD VYDLVSAEEC LRQAKYNEAQ GINRFSLVTS GRKPSPKNMK
     ELCVAARRMR RHSSIRLCAS LGLLDEEELQ ALYNAGVTRY HCNLETAPSH FDSLCTTHTQ
     EQKLKTLHAA RRVGMDLCCG GIIGMGETVE QRIEFAFTLR ELDIQSIPIN LLQPIPGTPL
     EHQSPLSEEE VLTTVALFRF INPTAYLRFA GGRSQLTPEA VRKSLYIGIN SAIVGDLLTT
     LGSKVSDDKE MILSEGYHFA DSQFDREHLW HPYTSTSNPL PVYKVKRADG VTITLASGQT
     LIEGMSSWWC AVHGYNHPAL NRAVQEQLSK MSHVMFGGLT HDPAIELGKL LLPLVPPSMQ
     KIFYADSGSV AVEVAMKMAV QYWYAAGQPE KSNFVTIRNG YHGDTWNAMS VCDPVTGMHS
     IFGSALPIRH FLPAPTSRFG DEWDPEDIRP LEQLLEKQSG KLAAFILEPI VQGAGGMRFY
     HPEYLRQAAR LCRQHGVLLI FDEIATGFGR TGKFFAWEHA GVEPDIMCIG KALTGGYMTL
     SAVLTTNEVA DCISNHFPGA FMHGPTFMGN PLACAVACAS IRLLLESGWQ ENVKRIEAQL
     NRELAPARKL PQVADVRVLG AIGVIEMKEP VNMAHLQRRF VEEGIWLRPF GKLVYVMPPF
     IITSEQLTKL TEGMIKCITD GSTCL
//