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
//