ID A0A0M2HM76_9MICO Unreviewed; 642 AA.
AC A0A0M2HM76;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:KJL45553.1};
DE EC=3.7.1.- {ECO:0000313|EMBL:KJL45553.1};
GN Name=iolD {ECO:0000313|EMBL:KJL45553.1};
GN ORFNames=RS81_00172 {ECO:0000313|EMBL:KJL45553.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL45553.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL45553.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL45553.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL45553.1}.
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DR EMBL; JYIZ01000020; KJL45553.1; -; Genomic_DNA.
DR RefSeq; WP_045274188.1; NZ_JYIZ01000020.1.
DR AlphaFoldDB; A0A0M2HM76; -.
DR STRING; 92835.RS81_00172; -.
DR PATRIC; fig|92835.4.peg.180; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000033956; 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; 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:KJL45553.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 226..359
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 422..590
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 642 AA; 68646 MW; CF2A69E1A9878D9B CRC64;
MTAMKRMTVS QALIEFLAHQ WTVDGDVRER TVPGVFGIFG HGNVAGIGQA LRQLNASEPD
LMPYRQARNE QAMVHQSVGW SRVHRRRSTW ASAASVGPGA TNMLTGAALA TTNRLPALLL
PSDTFATRVA DPVLQQLEQP FDTGLTVNDA FRPLSRFFDR VQRPEQLFST ALAAMRVLTD
PAETGAVTIA LPEDVQAEAL DVPLAFLQDR EWHIRRPVPE TAALGRAVAA IRAAERPFIV
AGGGVIYSGA EEQLRRFVEA TGIPVGTTQA GGGSLPWYHP QYLGAVGATG TTAANRLAAD
ADLVIGIGTR YSDFTTASRS AFQDPGVRFV NINVASFDAY KHGTQLPVIA DAREALAALA
AELVGFAVSP ALVERITREK GEWDAAVDAA FVPSGLERPG QPEIIGAVRA ATAPEDVIVQ
AAGSLPGDLH KLWRVADPLG YHVEYAYSCM GYEIAGGLGV KRGLEALGDD RDVVVMVGDG
SYLMLSSELA TAVAEGIKII VVLIQNHGYA SIGHLSETVG SERFGTKYRA YDADARNFQG
DQVLPVDLAM NARSYGLDVI EVSPGATAID DLRAAMATAK ASARSTLIHI ESDPLLYAPD
GEGWWDVPVP EASSLEATQA ARTEYEWGRT AQRPLLGDEG KR
//
