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Database: UniProt
Entry: A0A0M4LE96_9GAMM
LinkDB: A0A0M4LE96_9GAMM
Original site: A0A0M4LE96_9GAMM 
ID   A0A0M4LE96_9GAMM        Unreviewed;       618 AA.
AC   A0A0M4LE96;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:ALE01306.1};
GN   ORFNames=W908_01005 {ECO:0000313|EMBL:ALE01306.1};
OS   Candidatus Pseudothioglobus singularis PS1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX   NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01306.1, ECO:0000313|Proteomes:UP000068905};
RN   [1] {ECO:0000313|EMBL:ALE01306.1, ECO:0000313|Proteomes:UP000068905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS1 {ECO:0000313|EMBL:ALE01306.1,
RC   ECO:0000313|Proteomes:UP000068905};
RX   PubMed=26494659;
RA   Marshall K.T., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT   Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01155-e01115(2015).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP006911; ALE01306.1; -; Genomic_DNA.
DR   RefSeq; WP_053819592.1; NZ_CP006911.1.
DR   AlphaFoldDB; A0A0M4LE96; -.
DR   STRING; 1125411.W908_01005; -.
DR   KEGG; tsn:W908_01005; -.
DR   PATRIC; fig|1125411.7.peg.198; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000068905; 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:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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; 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:ALE01306.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068905};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..132
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          220..350
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          419..572
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          598..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  67353 MW;  97BC703F5D9134BC CRC64;
     MKTIRLTMTQ AIVKYLSSQF IETEEGIQPI FAGVFAIFGH GNVAGIGQAL NECQDKLPTY
     RGHSEQGMVH SAIAYAKANN RQRMMACTSS IGPGATNMVT AAALAHVNRL PVLLLPGDYF
     ASRTPDPVLQ QLEDFSDPTV SVNDCFRPVS RYFDRIMRPE QIINSLPVAI QTLLDPENCG
     PVTLSLPQDV QAEAFDYPEA FFKKRTHKIR KIKVDDDELN RAVDILKNSK KPLIIAGGGV
     HYAKACDVLK AFSKKYQIPV AETSAGKGAV TWDHPGYVGA IGVTGSSAAN NLAREADTVL
     AIGTRLNDFI SGSRALFSDK TLIQLNVARF DTIKHNAFSL WGDAKLGISN LDECLNEWKV
     SDNWFKEAEA EASNWNNYYD DITAINSSSA AEGSLPTDAQ VLGEVKRNGE ASDIVVCAAG
     SLPGELHKLW RTEQTGGYHS EYGFSCMGYE IAGGLGVKMA EPDREVIVLV GDGSYLMLNS
     ELATSIMLGH KIIAVILDNR GFSCINRLQN ATGNTSFNNL LKDCKSIDDG HPEINFAMHA
     QSLGANSEHV ENIDELAAAL NRARSSTKSY VISLVTDSHK ISPEGGCWWE VAVPEVSSNE
     KSEQILSSYK ESKTKQPY
//
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