ID   A0A4Q0U2X9_9BACE        Unreviewed;       745 AA.
AC   A0A4Q0U2X9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   16-OCT-2019, entry version 3.
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=bioB {ECO:0000256|HAMAP-Rule:MF_01694};
GN   Synonyms=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
GN   ORFNames=DBK98_08495 {ECO:0000313|EMBL:RXI13040.1};
OS   Bacteroides sp. PHL 2737.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=2162637 {ECO:0000313|EMBL:RXI13040.1, ECO:0000313|Proteomes:UP000289538};
RN   [1] {ECO:0000313|EMBL:RXI13040.1, ECO:0000313|Proteomes:UP000289538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHL 2737 {ECO:0000313|EMBL:RXI13040.1,
RC   ECO:0000313|Proteomes:UP000289538};
RA   Eshaghi A., Graham C., Kus J.V., Soares D., Patel S.N.;
RT   "Draft genome of multi-resistant B. fragilis.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin
CC       by the insertion of a sulfur atom into dethiobiotin via a radical-
CC       based 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
CC       (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
CC       animotransferase known to utilize SAM as an amino donor.
CC       {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-amino-7-oxononanoate + S-adenosyl-L-methionine = 7,8-
CC         diaminononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate;
CC         Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, ChEBI:CHEBI:57532,
CC         ChEBI:CHEBI:58500, ChEBI:CHEBI:59789; EC=2.6.1.62;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-SH + dethiobiotin + 2 reduced [2Fe-2S]-
CC         [ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine +
CC         [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-
CC         2S]-[ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:17319, ChEBI:CHEBI:29917,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57586,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57861, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64428; EC=2.8.1.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01694, ECO:0000256|SAAS:SAAS01122561};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
CC       7,8-diaminononanoate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01694,
CC       ECO:0000256|SAAS:SAAS00063342}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-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
CC       synthase family. {ECO:0000256|HAMAP-Rule:MF_01694}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RXI13040.1}.
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DR   EMBL; QAWD01000007; RXI13040.1; -; Genomic_DNA.
DR   RefSeq; WP_005809132.1; NZ_QAWD01000007.1.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000289538; Unassembled WGS sequence.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|HAMAP-Rule:MF_01694,
KW   ECO:0000256|SAAS:SAAS00448073};
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01694,
KW   ECO:0000256|SAAS:SAAS00448030};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01694,
KW   ECO:0000256|SAAS:SAAS00448045};
KW   Complete proteome {ECO:0000313|Proteomes:UP000289538};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00448063};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01694,
KW   ECO:0000256|SAAS:SAAS00448067};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01694,
KW   ECO:0000256|SAAS:SAAS00448059};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01694,
KW   ECO:0000256|SAAS:SAAS00448054};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01694,
KW   ECO:0000256|SAAS:SAAS00101389}.
FT   DOMAIN       52    257       Elp3. {ECO:0000259|SMART:SM00729}.
FT   DOMAIN      228    319       BATS. {ECO:0000259|SMART:SM00876}.
FT   REGION      428    429       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   REGION      625    626       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   METAL        62     62       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   METAL        66     66       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   METAL        69     69       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   METAL       106    106       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   METAL       138    138       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   METAL       198    198       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   METAL       268    268       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01694}.
FT   BINDING     368    368       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     461    461       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     562    562       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     591    591       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     624    624       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     708    708       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   SITE        333    333       Participates in the substrate recognition
FT                                with KAPA and in a stacking interaction
FT                                with the adenine ring of SAM.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   MOD_RES     591    591       N6-(pyridoxal phosphate)lysine.
FT                                {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
//