ID A0A4Q0U2X9_9BACE Unreviewed; 745 AA. AC A0A4Q0U2X9; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 22-FEB-2023, entry version 17. 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; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC 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 AlphaFoldDB; A0A4Q0U2X9; -. 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 CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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/MiaA/NifB-like_rSAM. 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 PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1. DR PANTHER; PTHR42684:SF17; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1. DR Pfam; PF00202; Aminotran_3; 1. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDG01278; biotin_synthase_like; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 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|HAMAP-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 //