ID C1HBL6_PARBA Unreviewed; 384 AA.
AC C1HBL6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=biotin synthase {ECO:0000256|ARBA:ARBA00012236};
DE EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236};
GN ORFNames=PAAG_08157 {ECO:0000313|EMBL:EEH38430.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH38430.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH38430.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR001619-1};
CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC cysteines and 1 arginine. {ECO:0000256|PIRSR:PIRSR001619-1};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR001619-1};
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|PIRSR:PIRSR001619-1};
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}.
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DR EMBL; KN294021; EEH38430.2; -; Genomic_DNA.
DR RefSeq; XP_002789903.2; XM_002789857.2.
DR AlphaFoldDB; C1HBL6; -.
DR STRING; 502779.C1HBL6; -.
DR GeneID; 9093149; -.
DR KEGG; pbl:PAAG_08157; -.
DR VEuPathDB; FungiDB:PAAG_08157; -.
DR eggNOG; KOG2900; Eukaryota.
DR HOGENOM; CLU_033172_3_2_1; -.
DR OMA; NICTTHT; -.
DR OrthoDB; 3682774at2759; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000002059; Partially assembled 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 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; 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; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF001619; Biotin_synth; 1.
DR SFLD; SFLDF00272; biotin_synthase; 1.
DR SFLD; SFLDG01278; biotin_synthase_like; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR001619-1};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR001619-1};
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR001619-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR001619-
KW 1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001619-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR001619-1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 85..314
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 144
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 177
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 237
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 309
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
SQ SEQUENCE 384 AA; 42135 MW; EE46A0BA0A01142B CRC64;
MASMRLSPLV RKSVRRTCGP ITQNRAATSI SPASASIPKA LQDALAAESP RINWTRDEIR
QIYDVPLHQL THAAAIVHRR FHDPSAIQLC TLMNIKVGGC TEDCSYCSQS SRYNTGLKAT
KMSPVDSVLE AARIAKENGS TRFCLGAAWR DMRGRKTSLR NIKEMISGVR KLDMEVCVTL
GMIDGDQARE LKEAGLTAYN HNVDTSREFY PSIITTRSYD ERLQTLSQVR EAGINVCSGG
ILGLGEEDSD RVGLLHAVAT LPAHPESFPV NALVPIKGTP LGDRKRIEFD KLLRTVATAR
IILPKTTVRL SAGRISMTEE QQVACFMAGA NSVFTGEKML TTDCNGWEED KKMFAKWGFY
PMQAYQRGEF RASSDAAAAV AAAS
//
