ID A0A136M2M2_9BACT Unreviewed; 612 AA.
AC A0A136M2M2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:KXK28126.1};
DE EC=3.7.1.- {ECO:0000313|EMBL:KXK28126.1};
GN Name=iolD {ECO:0000313|EMBL:KXK28126.1};
GN ORFNames=UZ16_OP3001003562 {ECO:0000313|EMBL:KXK28126.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK28126.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK28126.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK28126.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK28126.1}.
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DR EMBL; LMZT01000178; KXK28126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136M2M2; -.
DR STRING; 1617433.UZ16_OP3001003562; -.
DR PATRIC; fig|1617433.3.peg.3825; -.
DR Proteomes; UP000070296; Unassembled WGS sequence.
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; cd02003; TPP_IolD; 1.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KXK28126.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 2..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 211..345
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 408..566
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 612 AA; 66692 MW; ABA0B6FCD72E9D67 CRC64;
MAQALIGFLK NQFVERDGIQ NPFFGGCFGI FGHGNVAGVG EALQENPDFR YYQCRNEQAM
VHTASAYAKM SNRLRTIACT TSIGPGATNM LSGAALATVN RLPVLLLPGD IFAKRKVAPV
LQQLESEHTQ DISVNDCFRP VSRYWDRIYR PEQLITALPE AMRVLTSPAD TGAVTLALPQ
DTQTEAFDYP RELFEKRIWV IPRNRPDASL VNKALEWIRA AKRPLIIAGG GVHYSEANEI
LAQIAQATGI PVGETQAGKG SLHYQHPQSV GAIGVTGTSA ANILAESADL VIGVGTRYSD
FTTASKTAFQ APEVRFININ AAEFDAFKHN AIPLVGDARV ILAELHQNLA GWNVGSGYAD
KIEKLRTDWD NEVERLYNLG HQPLLSQSEV VGAVNTFSAP TDVMVCAAGS LPGDLHKLWR
TRDPRGYHLE YGYSCMGYEI AGGLGVKMAA PEKEVYVLLG DGSYLMMSTE IVTSIQEGCK
LIIVLLDNHG YASIGGLSAA CGSQGFGTRY KYRDSRGSIS GKDLPIDYAA NASSLGAISL
RAKNLDELKA ALATARDQDR TTVIVVETDI DERVPGYNSW WDVAVAEVSS IKSVQDARKK
YEESVQKERY FL
//
