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Database: UniProt
Entry: A0A9R0ZDP0_TRITD
LinkDB: A0A9R0ZDP0_TRITD
Original site: A0A9R0ZDP0_TRITD 
ID   A0A9R0ZDP0_TRITD        Unreviewed;       347 AA.
AC   A0A9R0ZDP0;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   RecName: Full=biotin synthase {ECO:0000256|ARBA:ARBA00012236};
DE            EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236};
GN   ORFNames=TRITD_7Av1G109440 {ECO:0000313|EMBL:VAI74596.1};
OS   Triticum turgidum subsp. durum (Durum wheat) (Triticum durum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4567 {ECO:0000313|EMBL:VAI74596.1, ECO:0000313|Proteomes:UP000324705};
RN   [1] {ECO:0000313|EMBL:VAI74596.1, ECO:0000313|Proteomes:UP000324705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Svevo {ECO:0000313|Proteomes:UP000324705};
RG   International Durum Wheat Genome Sequencing Consortium (IDWGSC);
RA   Milanesi L.;
RL   Submitted (SEP-2017) 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=[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|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}.
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DR   EMBL; LT934123; VAI74596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9R0ZDP0; -.
DR   Gramene; TRITD7Av1G109440.1; TRITD7Av1G109440.1; TRITD7Av1G109440.
DR   Proteomes; UP000324705; Chromosome 7A.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
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-KW.
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   InterPro; IPR058240; rSAM_sf.
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   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};
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:UP000324705};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          41..275
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         105
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT   BINDING         138
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT   BINDING         198
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT   BINDING         270
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
SQ   SEQUENCE   347 AA;  37990 MW;  2954C99CF1254A91 CRC64;
     MMLLLARSLR SRLCPPLASA VSAAPFSSVS AAAAEAERAV RDGPRNDWTR PEIQAIYDSP
     LLDLLFHGAQ SSRYSTGLKA EKLMKKDAVL EAAKKAKEAG STRFCMGAAW RETIGRKTNF
     NQILEYVKDI RGMGMEVCCT LGMLEKQQAE ELKKAGLTAY NHNLDTSREY YPNIISTRSY
     DDRLQTLQHV REAGISVCSG GIIGLGEAEE DRVGLLHTLA TLPTHPESVP INALIAVKGT
     PLQDQKPVEI WEMIRMIASA RIVMPKAMVR LSAGRVRFSM PEQALCFLAG ANSIFAGEKL
     LTTANNDFDA DQAMFKILGL IPKAPNFGDE EVMVAAPTER CEQAALM
//
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