ID F5YMA5_TREPZ Unreviewed; 625 AA.
AC F5YMA5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Probable malonic semialdehyde oxidative decarboxylase {ECO:0000313|EMBL:AEF84742.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:AEF84742.1};
GN OrderedLocusNames=TREPR_0397 {ECO:0000313|EMBL:AEF84742.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84742.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF84742.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001843; AEF84742.1; -; Genomic_DNA.
DR RefSeq; WP_015709614.1; NC_015578.1.
DR AlphaFoldDB; F5YMA5; -.
DR STRING; 545694.TREPR_0397; -.
DR KEGG; tpi:TREPR_0397; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_12; -.
DR OMA; PNTYHLE; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000009223; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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 Oxidoreductase {ECO:0000313|EMBL:AEF84742.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 219..353
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 421..580
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 625 AA; 68363 MW; B90BCA1C6C60552F CRC64;
MKTVRLTMAQ ALLRFLDNQY IEVDGEEIKY VHGVFGIFGH GVVVGLGEAL AAKDHGLRFY
QGKNEQGAGH AAMGFAKQNN RRRIMAVCSS IGPGALNMVT AAGTATVNRI PVLFLPGDAF
ACRQPDPVLQ QVESPYDYTN TASDAFRAVS RYWDRVQRPE QLMTAMINAF RVLTDPADTG
AVTVALPQDV QGEAYDYPEE FLAKRVHHIE RRIPTKGQID RASALLKAAK KPMVICGGGV
RFSGAGKELE NFCKTYHIPF GETQAGKGTI LWDNPYNLSG IGNTGALSAN RIAKEADLII
AVGTRLGDFT TCSKWLFQHP DARIMGINVA SFDAYKMNGE PIIADAKLTL EALTKAAPGY
KSTWGDRIQQ VRDEWKAEVD RLYSEDAEPA PDGSPLLSQA RVLGELNDRL LPKDTIVVSG
SGSIPSDMQR VWRARTEDTY HMEYGFSCMG YEVAAALGAK IAFPDKEIVA LVGDGAYTML
HTELLTAVQE GRKIIVVVLD NAGFHCIDNL QHSQGIVHFG NEWKTRDDKS GRLEGASVQV
DYAKNGESWG ALGLRARTPA ELEKAVKEAL ASKKSVVIDV KTSAKTMTHG YESWWRVGTA
QVSTNPEVEK AAKEMAAEVT KARKY
//