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Database: UniProt
Entry: A6WFD0_KINRD
LinkDB: A6WFD0_KINRD
Original site: A6WFD0_KINRD 
ID   A6WFD0_KINRD            Unreviewed;       643 AA.
AC   A6WFD0;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:ABS05519.1};
GN   OrderedLocusNames=Krad_4056 {ECO:0000313|EMBL:ABS05519.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS05519.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA   Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000750; ABS05519.1; -; Genomic_DNA.
DR   RefSeq; WP_012086193.1; NC_009664.2.
DR   AlphaFoldDB; A6WFD0; -.
DR   STRING; 266940.Krad_4056; -.
DR   KEGG; kra:Krad_4056; -.
DR   eggNOG; COG3962; Bacteria.
DR   HOGENOM; CLU_013748_6_0_11; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000001116; 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: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; 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   Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          18..154
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          239..373
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          439..595
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   643 AA;  69063 MW;  37601064FD06B662 CRC64;
     MSAVPPNPAV VTVRLTVSQA VVRFLQAQFS ERDGVRRPFF GGVFGIFGHG NVAGIGQALL
     EAEEGALGDD WEPPAHLRYM TGRNEQAMVH AAVGYARQQD RLQTLAVTAS VGPGSTNMLT
     GAALATVNRI PVLLLPADVF ATRVASPVLQ ELEQPYGYDV SVNDAFRPLS KFFDRVWRPE
     QLPSALLGAM RVLTDPAETG AATICLPEDL QAEAWDFPVE LFRERTWRIA RPVPEKVAIA
     EAADLIRSAK APLVVAGGGV VYSQATEALR AFVEATGIPV GQSQAGKGAI RYDHPLSLGA
     VGSTGTTAAN EIAAEADVVI GIGTRYSDFT TGSRTAFQNP DVRFVNVNVA SLDAVKHAGL
     PVQADAREAL EALTEALEGF STPDAYRERA ARLNREWDAV VDRFFHSGIG EAKGLLAQAE
     VIGAVDEVAG DRDVVVCAAG SLPGDLHAMW RSRDPKQYHV EYGYSCMGYE IPGGIGVALA
     APDRDVFITV GDGSFLMMPT ELVTAVQEGV KVIVVLLQNH GFASIGALSE QHGSQRYGTR
     YRKRSESGRL EGEKLPVDLA ANVESLGIRT LRAGTRKELV AALQDAKASR ESTCVYVETD
     LYSEAPDGGG WWDVPVSEVS HLESTRAART WYEGEKRTQR PLL
//
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