ID A0A139H3V9_9PEZI Unreviewed; 1126 AA.
AC A0A139H3V9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=biotin synthase {ECO:0000256|ARBA:ARBA00012236};
DE EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236};
GN ORFNames=AC579_1318 {ECO:0000313|EMBL:KXS97111.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXS97111.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXS97111.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXS97111.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC family. {ECO:0000256|ARBA:ARBA00010765}.
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:KXS97111.1}.
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DR EMBL; LFZO01000800; KXS97111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139H3V9; -.
DR STRING; 113226.A0A139H3V9; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000073492; Unassembled WGS sequence.
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: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; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR HAMAP; MF_01694; BioB; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR002684; Biotin_synth/BioAB.
DR InterPro; IPR024177; Biotin_synthase.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR000195; Rab-GAP-TBC_dom.
DR InterPro; IPR035969; Rab-GAP_TBC_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; PF00566; RabGAP-TBC; 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 SMART; SM00164; TBC; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50086; TBC_RABGAP; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 97..328
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 452..701
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000259|PROSITE:PS50086"
FT REGION 943..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1126 AA; 124709 MW; A9B68835A4A42703 CRC64;
MSLTVLSRRA AARSVHPATA VFNRQFSTPV NDTFSPLSSS STPPPPPEAQ SALWNAVNAR
APRYDWTKDE IRDIYNTPLM ELAHQSGFLH RRFHSPSAVQ MCTLMNIKTG GCSEDCSYCA
QSSRYNTGLK ATKMSPVDDV LNAARIAKSN GSTRFCMGAA WRDMRGRKTS LKNVKAMVEG
IRAMDMEVCV TLGMIDQSQA DELKEAGLTA YNHNVDTSRE HYPSVITTRS YDERLQTLSN
VRNAGINVCS GGILGLGEKP EDHVGLIYTV STLPAHPESF PVNALVPIKG TPLGDSNKKR
ISFDAILRTI ATARLVMPAT IIRIAAGRTT MSEAEQILCF SAGANAVFTG EKMLTTEAVG
WDTDKVMFEK YGLVPMKPFE RGAYRETSWS WNGDSGCTYT SLGSRDSGTA RGPALRTDGW
ASAARPNWQK LAQYKTLREL KHGVRLDEHS SAATSGLRSI CWKAFLLFDS LDVEDWQRTL
ASSRSAYNSL RAHFFRHIDN PEEIGSDFDP LTQDAESSPW QQLKKDEELR AEIVQDVERQ
SILQMPSHRR MLTDMLFTYC KLNPDVGYRQ GMHEIAAPIL WVVEGDAVDV GEASKTLGEE
AIIKDVFDPE FIEHDSFAIF GQVMQSAKTF YISEGPVSIA TRSKHIFNEL MVQIDPDLVK
HLESLDVLPQ VFLIRWIRLL FGREFEFESV LALWDVIFAE DASLELVDHI CLAMLLRIRW
HLLDADYNNA LGLLLRYPDL DKDLPAQSLG LDAVYLRDHM NAEGSSYLVL KYTGRPLTSS
NRPTTPPALQ RNITQFSGLN AVRHSKPSRN NIEAVLQSTA KNLFAQSERL GIGKAVRNTI
DDIHKKAQEI RDSQAPSPPP WRRSGTPRVL GRLRDMEERN KRLSVLLGQA VNELWECQGL
VSGDQKTSDG SSQEANVEKL SAAIARVQFV HVYLDQPTLI LPTEDDTTQE SGNGTTKSVA
SPQQGPELDP DHPTAESTVL PPTNDSVTGQ AEAPSHRLAL ADPSTLEDFH DSEAQTDVKL
EPPASELKAD PDNTPVKSST PRPSLEQSPF SFMLGQDTTL NEGQDRKRVP PPSQDRGNAS
LFGNDKATHR TPSHTPTGSV NKFLADDGGK DEFDFGSLRR GKGPKR
//
