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Database: UniProt
Entry: A0A2U1MPY1_ARTAN
LinkDB: A0A2U1MPY1_ARTAN
Original site: A0A2U1MPY1_ARTAN 
ID   A0A2U1MPY1_ARTAN        Unreviewed;       376 AA.
AC   A0A2U1MPY1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=biotin synthase {ECO:0000256|ARBA:ARBA00012236};
DE            EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236};
GN   ORFNames=CTI12_AA325490 {ECO:0000313|EMBL:PWA63310.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA63310.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA63310.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA63310.1};
RX   PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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}.
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:PWA63310.1}.
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DR   EMBL; PKPP01004667; PWA63310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1MPY1; -.
DR   STRING; 35608.A0A2U1MPY1; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000245207; 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   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:UP000245207};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRSR:PIRSR001619-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          77..306
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         92
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         96
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         99
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         136
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT   BINDING         169
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT   BINDING         229
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
FT   BINDING         301
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001619-1"
SQ   SEQUENCE   376 AA;  41562 MW;  5F6268DB76D53C04 CRC64;
     MILIRSIRRS FPSSSIIPCL QRRSVSSSSA AVEADRTIRQ GPRNDWKKEE IKSVYDSPLL
     DLLFHGAQVH RHAHNFREVQ QCTLLSVKTG GCSEDCSYCP QSSRYDTGVK AQKLMNKDAV
     LEAAQKAKEA GSTRFCMGAA WRDTIGRKTN FSQILEYVKD IRGMGMEVCC TLGMIEKQQA
     LELKKAGLTA YNHNLDTSRE YYPNVITTRT YDERLETIKH VRDAGINVCS GGIIGLGEAE
     EDRVGLLHTL ATLPSHPESV PINALLAVKG TPLEDQKEVE IWEMIRMIAT ARITMPKAMV
     RLSAGRVKFS VPEQALCFLA GANSIFTGEK LLTTPNNDFD ADQSMFKLLG LIPKPPSFSD
     EAGEVEPCQE AVSSSS
//
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