ID A0A364KP20_9EURO Unreviewed; 1264 AA.
AC A0A364KP20;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=biotin synthase {ECO:0000256|ARBA:ARBA00012236};
DE EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236};
GN ORFNames=BHQ10_001287 {ECO:0000313|EMBL:RAO65275.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO65275.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO65275.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO65275.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 2/2. {ECO:0000256|ARBA:ARBA00004942}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC family. {ECO:0000256|ARBA:ARBA00010765}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000256|ARBA:ARBA00005964}.
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:RAO65275.1}.
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DR EMBL; MIKG01000001; RAO65275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364KP20; -.
DR STRING; 1196081.A0A364KP20; -.
DR OrthoDB; 3682774at2759; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0004076; F:biotin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR HAMAP; MF_01694; BioB; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR002684; Biotin_synth/BioAB.
DR InterPro; IPR024177; Biotin_synthase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00433; bioB; 1.
DR PANTHER; PTHR22976; BIOTIN SYNTHASE; 1.
DR PANTHER; PTHR22976:SF2; BIOTIN SYNTHASE, MITOCHONDRIAL; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00272; biotin_synthase; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 959..1188
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 140502 MW; 27F58F06E1AC37DD CRC64;
MTTKIGQNAD ITKASPTDAP PESASIHEGK FPDAKAVDIV HAAEEEFTEE QYRKLVRKVD
LILLPLMWIA SGTQYADKAS ISTQSTFGIT QDTHLVGQQY SWLTSIFYIA FLVAEAPGSY
ILQKANINYT VSTCMFIWGI LVLCIAFAKN FTDLMVLRFL QGVAECTTYP ALLIMTAAWY
TREEHAMRAV IWGSANSGMD ILTSLINYSI GTRAKSHPGG LAPWKGISFF LGSLTIVISV
FAFFLFGTPR EVRWLSETEK RMAYARVVKS QTGSDAQKRN ISWRQVLETF KDPQTYFFFF
IVLINSIPNG GTTSFGNLVY VSFGFTALET ITEGKIPQQA LSIICLLSAG YLTLKKPGLR
LYISMISVVP AFVGMLALAL LPKRGHLWTR WGMYFITIVG NVAGPRTIKG VQYDNKARRY
AGIPYALPPT GDHRWRKPRS LPSSYTYTQP DGTPLNASGF RAVCPQATFH SGAEQGLDQE
KYTEDCLILN FWTPVPRDEQ QNKRNWPVML WLHGGWFQMG NPCQELGMDP TEMISTGKLN
AIVVGIGYRL NIFGFLAGEA LLQESNGECA GNMGLWDQRL AMEWVKEYIG AFGGDSDNIT
LAGRSAGAYA VHAQTLHDFR TKNTQALYHR IFMCSNAISA QPKTVAETQP QFDEVCKHFN
VPSTLTGLEK LSQLRKISSD DLVNAIKNLQ HHTFRPVTDG IFIHAGLIDY QTGPEFAQEF
KQRNLKLLIG EVLNEETLYS TYNAPEPNKE SLSLQVSNYY APATTERILQ HYSFPKSTDP
NEWRTTYGNI VADGQVRAPS RSLANSLFEH GVAMSDLWRY QIAYRLSFID DKVAPLSFGV
AHAMDKPLWN FAIVHGPTPK DREIMEEWVA ILVAFVNNDP TYRFGTTSIR ELKVLTSEGG
APVSPWISSA IPAVVKNATA TQVPRTTWTR DEVRQVYETP LSQLTHAAAI VHRRFHDPAA
IQMCTLMNIK TGGCSEDCSY CAQSSRYNTG LKATRLSPLE EVLQAARIAK ENGSTRFCMG
AAWRDMRGRK TSLKNIKEMV TGVRSMGLEV CVTLGMIDTE QAKELKDAGL TAYNHNLDTS
REYYPSIITS RSYDERLQTL SNVRDAGINV CSGGILGLGE ADSDRIGLLH TVATLPSHPE
SFPVNALVPI KGTPLGDRKM ISFDKLLRTI ATARIVLPTT IVRLAAGRIN LSEEQQVTCF
MAGANAVFTG EKMLTTDCNG WDQDHEMFRK WGFYPMKSFE NEEVKGTKSA VITESDSGMV
AASI
//
