ID A0A6A1KAS5_9BACE Unreviewed; 813 AA. AC A0A6A1KAS5; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 07-APR-2021, entry version 4. 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=F2Y25_04830 {ECO:0000313|EMBL:KAA5493922.1}, F2Y27_06810 GN {ECO:0000313|EMBL:KAA5482182.1}, F2Y47_11270 GN {ECO:0000313|EMBL:KAA5503271.1}; OS Bacteroides caccae. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=47678 {ECO:0000313|EMBL:KAA5493922.1, ECO:0000313|Proteomes:UP000386011}; RN [1] {ECO:0000313|Proteomes:UP000386011, ECO:0000313|Proteomes:UP000400403, ECO:0000313|Proteomes:UP000460172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIOML-A20 {ECO:0000313|EMBL:KAA5503271.1, RC ECO:0000313|Proteomes:UP000460172}, BIOML-A22 RC {ECO:0000313|EMBL:KAA5493922.1, ECO:0000313|Proteomes:UP000386011}, RC and BIOML-A23 {ECO:0000313|EMBL:KAA5482182.1, RC ECO:0000313|Proteomes:UP000400403}; RX PubMed=31477907; DOI=.1038/s41591-019-0559-3; RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X., RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D., RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J., RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A., RA Xavier R.J., Alm E.J.; RT "A library of human gut bacterial isolates paired with longitudinal RT multiomics data enables mechanistic microbiome research."; RL Nat. Med. 25:1442-1452(2019). 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=(S)-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:ARBA00023342, CC ECO:0000256|HAMAP-Rule:MF_00834}; 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; 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAA5493922.1}. 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; VVYH01000005; KAA5482182.1; -; Genomic_DNA. DR EMBL; VVYG01000004; KAA5493922.1; -; Genomic_DNA. DR EMBL; VVYE01000010; KAA5503271.1; -; Genomic_DNA. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000386011; Unassembled WGS sequence. DR Proteomes; UP000400403; Unassembled WGS sequence. DR Proteomes; UP000460172; 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|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, ECO:0000313|EMBL:KAA5493922.1}; 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}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000313|EMBL:KAA5493922.1}. FT DOMAIN 115..320 FT /note="Elp3" FT /evidence="ECO:0000259|SMART:SM00729" FT DOMAIN 291..382 FT /note="BATS" FT /evidence="ECO:0000259|SMART:SM00876" FT REGION 491..492 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT REGION 688..689 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT METAL 125 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694" FT METAL 129 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694" FT METAL 132 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694" FT METAL 169 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694" FT METAL 201 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694" FT METAL 261 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694" FT METAL 331 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694" FT BINDING 431 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 524 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 625 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 654 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 687 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 771 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT SITE 396 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 654 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" SQ SEQUENCE 813 AA; 90694 MW; BA0E1E12BA7269BB CRC64; MKKQRHIQTT RTLLSRFRYW GRKNYAAFAS MGREFQIGHL HTNVVDVALR KQNAAQTIPY HTFMTLQEIK DQVLAGIDIS PDQAAWLANM ADSEALYAAA HEITVARASH EFDMCSIINA KSGRCPENCK WCAQSSHYKT QAEVYDLLPA KECLRQAKYN ETQDVNRFSL VTSGRKPSSR QITQLCDTVR HIRRHSSIQL CASLGLLDEN ELHALHDAGI TRYHCNLETA PSYFPKLCST HTQEQKLATL NAARRVGMDI CCGGIIGMGE TMEQRIEFAF TLKALNVQSI PINLLSPIPG TPLENEKPLS EEEVLRTIAL FRFINPTAFL RFAGGRSQLS SEAMSKALYI GINSAIVGDL LTTLGSKVSE DKQMILKEGY QFASSQFDRE HLWHPYTSTT DPLPVYKVKR ADGATITLEN GRTLIEGMSS WWCAVHGYNH PALNQAAKDQ LDKMSHVMFG GLTHDPAIEL GKLLLPLVPP SMQKIFYADS GSVAVEVALK MAVQYWYAAG KPDKNNFVTI RSGYHGDTWN AMSVCDPVTG MHSLFGASLP VRYFVPAPSS RFDGEWNPQD IEPLRKTIEK HSEELAALIL EPIVQGAGGM WFYHPQYLRE AEKLCKEHGL LLIFDEIATG FGRTGKLFAW EYAGVEPDIM CIGKALTGGY MTLSAVLASN HVADTISNHA PGAFMHGPTF MGNPLACAVA CASVRLLLQS GWQENVKRIE TQLKEELTPA RELPQVADVR ILGAIGVIEM KRPVNMAFMQ RRFVEEGIWI RPFGKLVYLM PPFIITPEQL SKLTTGLLKV ISGERNKIYI NNL //