ID V6JU87_STRNV Unreviewed; 628 AA.
AC V6JU87;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:EST23278.1};
GN ORFNames=M877_27540 {ECO:0000313|EMBL:EST23278.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST23278.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST23278.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST23278.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:EST23278.1}.
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DR EMBL; AWQW01000198; EST23278.1; -; Genomic_DNA.
DR RefSeq; WP_023541608.1; NZ_CM002280.1.
DR AlphaFoldDB; V6JU87; -.
DR STRING; 193462.BBN63_23065; -.
DR PATRIC; fig|1352941.4.peg.5601; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_11; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000017971; 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:EST23278.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..353
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 417..577
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 628 AA; 67239 MW; 733CB3D38A5BDD60 CRC64;
MSTRRLTVAQ ALIAFLSRQY TERDGNRRRL IDATWGIFGH GNVAGIGQAL VQAGPEMPYF
QGRSEQAMVH AAVGFARQSN RLATHAVTTS IGPGATNLVT GAALATINRL PVLLLPGDIF
ATHPADPVLQ QLEVPHAGDI SVNDALRPVS KYFDRVSRPE ALVPAALAAM RVLTDPAETG
AVTLALPQDV QAEAYDWPEE FFAERVWRVR RQGPDPYELA DAAEAVRAAR RPLLVAGGGV
HHSAAEDALA ALATATGIPV ASTQAGKGSL RHDHPADVGG IGHTGTATAD ELARTADLVI
GVGTRWSDFS TASATLFAHP SVRFLNINIT GFDAHKLAAS PLVADARTAL EDLTTALTGH
RVDAAYAAEY TQDKERWEHR VDAAFDTAED LVRPTQPQVL GLLDALVTDE DIVINAAGSL
PGDLHKLWRA RSRDQYHVEY GYSCMGYEIP AAIGVLLADP GRPVWALVGD GTYLMNPTEI
VTAVQERLPL KLVILQNHGY ASIGGLSESV GAERFGTAYR YREADTIGSP TYTGDPLPVD
LAANAASLGM RVIRAKTIRD LREALAVARE SDVPTCVYAE TETADTVSGA PPAQAWWDVP
VAETATRPSA VTAREEYDRK AAARRRHL
//