ID A0A2P7YZF7_9ASCO Unreviewed; 930 AA.
AC A0A2P7YZF7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Biotin synthase {ECO:0000313|EMBL:PSK41343.1};
GN ORFNames=C7M61_001025 {ECO:0000313|EMBL:PSK41343.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK41343.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK41343.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK41343.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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.
CC {ECO:0000256|ARBA:ARBA00004746}.
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:PSK41343.1}.
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DR EMBL; PYFQ01000001; PSK41343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YZF7; -.
DR STRING; 418784.A0A2P7YZF7; -.
DR EnsemblFungi; C7M61_001025_t1; PSK41343.1; C7M61_001025.
DR VEuPathDB; FungiDB:C7M61_001025; -.
DR OrthoDB; 1664005at2759; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 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; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00433; bioB; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF117; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 1.
DR SFLD; SFLDF00272; biotin_synthase; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51387; FAD_PCMH; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 79..309
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 496..673
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 930 AA; 103047 MW; ABB3C96F0772FE5C CRC64;
MFIRKLATSA TLGSAKTLGV KAAFSEPSIV SPVKAINLAI NCKPHSKWTK QEIKEIYNTP
LLELTFQAQL QHRRYHDPAE VQLCTLLNIK TGGCSEDCKY CSQSSRYDTG TKAEKLVKLE
EVQKAAIKAK ENGSTRFCMG AAWRDMQGRK SGLKKIAEMV KWINDELKME TCVTLGMVNE
DQAKVLKDSG LTAYNHNIDT SREHYPSVIS TRTYDDRLET IKNVQKAGIK ACTGGILGLG
ETPDDHVSFL YTLATMERHP ESLPINRLVP IKGTPMEAEI SKLPIGSERR LKFDAILRTI
ATARLIMPES IIRLAAGRYT MKEHEQFLCF SAGCNAIFTG ERMLTTMCSG WEEDIAMLKK
WGMKPMKSFR KHGIEAAENV FQKGVETYPE NTSPTLKASS KATSILPALV AAVSLGSAGY
YLGRKRAIND PPEYAFPWSS TTKLELIDSP KYSTEEELRT AIDEIKRAVG DDHVTQSPAE
ITGHTDNGFT PHPPKPHEKP KYIVYAYSTE EVSKILKVAH KYNVPVVPYS GGSSLEGHTF
STRCGIILNT SRMNKVLQIN HDDLDATLQA GVNWVDLNEQ LTGEKMMFGC DCGPSGLIGG
MVNTNASGIN ASRYGAMVHN VISLTVVLAD GTVIKTRQRP RKTSSGYNLT GLFIGSEGTL
GIVTEATVKL QVKPQHETVA VGQFPSVLLA SQTVAELFKR GIRPEAIELL DEDMMHCTNY
SGQLSKKWLE VPTIFFKVGG LNKRVVDETL EIVRKVSLEN QCADFIIAKD KTEGDELFAA
RKNAFFSILD YGKNEIDEDV RLWVTDIAVP LSRLPKVVDE IRELVVKSGF QSVILGHVGD
GNLHADLFYK PDQLHECHKV INEITMIGLR NEGTASGEHG IGNGKRQFLS IELGQDAVDT
MRKLKLSLDP KRILNPDKIF KIDPHDEGEY
//
