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Database: UniProt
Entry: B4V9G4_9ACTN
LinkDB: B4V9G4_9ACTN
Original site: B4V9G4_9ACTN 
ID   B4V9G4_9ACTN            Unreviewed;       622 AA.
AC   B4V9G4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:AKL66201.1};
DE   SubName: Full=IolD protein {ECO:0000313|EMBL:EDX24601.1};
GN   ORFNames=M444_13165 {ECO:0000313|EMBL:AKL66201.1}, SSAG_04209
GN   {ECO:0000313|EMBL:EDX24601.1};
OS   Streptomyces sp. Mg1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX24601.1, ECO:0000313|Proteomes:UP000005764};
RN   [1] {ECO:0000313|EMBL:EDX24601.1, ECO:0000313|Proteomes:UP000005764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:EDX24601.1,
RC   ECO:0000313|Proteomes:UP000005764};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., Straight P.,
RA   Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA   Lander E., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. Mg1.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKL66201.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL66201.1,
RC   ECO:0000313|Proteomes:UP000035653};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT   Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
RN   [3] {ECO:0000313|EMBL:AKL66201.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL66201.1};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP011664; AKL66201.1; -; Genomic_DNA.
DR   EMBL; DS570412; EDX24601.1; -; Genomic_DNA.
DR   RefSeq; WP_008741623.1; NZ_DS570412.1.
DR   AlphaFoldDB; B4V9G4; -.
DR   STRING; 465541.M444_13165; -.
DR   KEGG; strm:M444_13165; -.
DR   PATRIC; fig|465541.12.peg.2862; -.
DR   eggNOG; COG3962; Bacteria.
DR   HOGENOM; CLU_013748_6_0_11; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000005764; Unassembled WGS sequence.
DR   Proteomes; UP000035653; Chromosome.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_IolD.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR   PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AKL66201.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..123
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          218..351
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          415..571
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   622 AA;  66188 MW;  C6953C23107A5B7D CRC64;
     MRLTVAQALV RFLARQYTER DGQRHRLIAA TWGIFGHGNV AGIGQALLET GHEEMPFLQG
     RNEQAMVHAA VGFARQSGRL SAHAVTTSIG PGATNLVTGA ALATINRIPV LLLPGDSFAT
     RPADPVLQQL EVPYAGDISV NDTLRPVSRF FDRVMRPEAL IPAALQAVRV LTDPVQTGAV
     TLALPQDVQA EAWEWPEEFF RERVWGVRRP RPDAAELAEA AEAVRGSARP LLIAGGGIRH
     SGAQAALAEF AEATGIPVAT TQAGKGALPY DHPAEVGGVG HTGTGTADGL AREADLVIAA
     GTRLTDFTTA SATLFQNPAV RFLGLNLDPF DAHKLAARPL VSDAREGLEE LRRAVAGYHV
     DTAYESTYKE RKRLWEERVD RAYAASGEDD APTQAQVLGL LDALVDDGDI LINAAGSLPG
     DLHKLWRARS ADQYHVEYGY SCMGYEIPAA IGVALAAPGR PVWALVGDGT YLMNPTEIVT
     AVQEGIAVKL VILDNHGYAS IGGLSGAVGG EGFGTAYRFR AVDGMYSGAP LPVDLAANAA
     SLGMAVIRTR TIGDLRKALA EARAADRPTC VYAQTRTPDT VSGPPPAQAW WDVPVAETAT
     RAAAALAREE YDRQAAQRRR HL
//
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