ID   F7NLR8_9FIRM            Unreviewed;       620 AA.
AC   F7NLR8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Myo-inositol catabolism protein IolD {ECO:0000313|EMBL:EGO63009.1};
GN   ORFNames=ALO_15212 {ECO:0000313|EMBL:EGO63009.1};
OS   Acetonema longum DSM 6540.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Acetonema.
OX   NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO63009.1, ECO:0000313|Proteomes:UP000003240};
RN   [1] {ECO:0000313|EMBL:EGO63009.1, ECO:0000313|Proteomes:UP000003240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO63009.1,
RC   ECO:0000313|Proteomes:UP000003240};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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:EGO63009.1}.
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DR   EMBL; AFGF01000144; EGO63009.1; -; Genomic_DNA.
DR   RefSeq; WP_004097102.1; NZ_AFGF01000144.1.
DR   AlphaFoldDB; F7NLR8; -.
DR   STRING; 1009370.ALO_15212; -.
DR   eggNOG; COG3962; Bacteria.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000003240; 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   Reference proteome {ECO:0000313|Proteomes:UP000003240};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..131
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          227..352
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          416..575
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   620 AA;  67324 MW;  6ABD8E32F8754DA4 CRC64;
     METMRLTMGQ ALLKFLDNQY VEFDGVVNKF VKGVFTLFGH GIVVGFGEAL ERYQGDMAVY
     QGKNEQGMAH AAIGYAKQKN RREIIACTSS IGPGALNMVT AAATATVNRI PLLLLPGDTF
     ACRQPDPVLQ QVENPSSLSI TANDAFKPVS RYWDRVVRPE QLMTAMIHAM RVLTDPADTG
     AVAICLPQDA EGEAYDYPVE FFARRVHHIA RRIPTRSELE HAVAKTITKK KPLLICGGGV
     VYSEAGDALI EFAEKFRIPF CETQAGKGAA PWNHGLNLGG VGVTGGLAAN RVAAAADLVI
     AVGTRLSDFT TASKWLFQNP DVDFLTINVN AFDACKMNAM TVIADAREGL QAFGAALEAA
     GYQSVYSGEI ETAKAEWDRE VDRLCSIDLA QGLSQTRALG EIAKMIGEDA VIVGSAGSLP
     GDLQRLWRPV KPKTYHMEYG FSCMGYEINA ALGVKMAEPQ REVYAMAGDG SYLMLHSELL
     TSIQEGYKIN VLLFDNCGFG CIENLQNSKG IPSFCTQTKF RDPATGRLTG RDMPVSYAEC
     AGGYGAKTYT ARTIEELKAS LASAKKDTVS TLIDIKVLPG TMTDGYESWW RVGVPEVSEN
     PDVVKAHELL VKEVSKTKKF
//