ID A0A4Q0U2X9_9BACE Unreviewed; 745 AA. AC A0A4Q0U2X9; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. 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}. 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; QAWD01000007; RXI13040.1; -; Genomic_DNA. DR RefSeq; WP_005809132.1; NZ_QAWD01000007.1. DR UniPathway; UPA00078; UER00160. DR Proteomes; UP000289538; Unassembled WGS sequence. 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 //