ID B1XTF2_POLNS Unreviewed; 601 AA.
AC B1XTF2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Thiamine pyrophosphate protein TPP binding domain protein {ECO:0000313|EMBL:ACB43629.1};
GN OrderedLocusNames=Pnec_0337 {ECO:0000313|EMBL:ACB43629.1};
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB43629.1};
RN [1] {ECO:0000313|EMBL:ACB43629.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1 {ECO:0000313|EMBL:ACB43629.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.;
RT "Complete sequence of Polynucleobacter necessarius STIR1.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001010; ACB43629.1; -; Genomic_DNA.
DR AlphaFoldDB; B1XTF2; -.
DR STRING; 452638.Pnec_0337; -.
DR KEGG; pne:Pnec_0337; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_3_4; -.
DR OrthoDB; 9785953at2; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 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; 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 PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 601 AA; 66633 MW; 9AA6722A98C45598 CRC64;
MKLSDYVAQK VVENGVKHVF MVTGGGAMHL NHSFGTRKDL ECIFNHHEQA CAIGAEAYYR
LTNRLPIVNV TSGPGGTNAI TGVYGAFVDS VAMLVISGQV KWETTVRSTG LPLRQYGDQE
LDIEELVRPV TKYCEMVTDP QTIRYHLEKA IYLAQSGRPG PCWLDIPLNV QGAQIDPDAL
VGFDPAELEE PWKKTDLKRV SKDILDKVRA AKRPVVFVGG GIRLSGEHKS FLKLVEKLQI
PVVTGWNAHD VIWNSHPNYA GRPGTIGDRA GNFVTQNADL LLVLGSRLNI RQVSYNWQSF
AREAFKIWVD IDELELKKPS VKADMPIHAN LKDLLPILAG ARYEGATPEH KEWMEWSKER
MRRFPTVLPE YRENNRVNPY CFVDELFKQL KDDQIVVTGN GSACVVSFQA ADLKPGQRLW
TNSGCATMGY DLPASIGAHK ASGGKSIVCL AGDGSIMMNL QELQTIAGNQ IPVKIFILNN
SGYVSIFQTH RNFFNGVEVG GGPKSGVTFP SFEKLSAAFD LPYLRVENHS QMQDAIEATL
QEVGPCVCEI MIDESVVFAP KLGAKQHPDG RITSPPLEDL SPFLSREVLR ENMTIESPQE
E
//
