ID A0A243WAQ3_9BACT Unreviewed; 589 AA.
AC A0A243WAQ3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Thiamine pyrophosphate-requiring protein {ECO:0000313|EMBL:OUJ71929.1};
GN ORFNames=BXP70_20095 {ECO:0000313|EMBL:OUJ71929.1};
OS Hymenobacter crusticola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1770526 {ECO:0000313|EMBL:OUJ71929.1, ECO:0000313|Proteomes:UP000194873};
RN [1] {ECO:0000313|EMBL:OUJ71929.1, ECO:0000313|Proteomes:UP000194873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIMBbqt21 {ECO:0000313|EMBL:OUJ71929.1};
RA Liang Y., Feng F.;
RT "A new Hymenobacter.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUJ71929.1}.
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DR EMBL; MTSE01000013; OUJ71929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243WAQ3; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000194873; Unassembled WGS sequence.
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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 Reference proteome {ECO:0000313|Proteomes:UP000194873};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 589 AA; 64584 MW; CF31E6D8A51D1373 CRC64;
MSQTVSEFLI QRLSAWGIKR IFGYPGDGIN GLMGALRKAK DHMEFIQVRH EEMASLMACA
HAKFTGEVGV CMATSGPGAI HLLNGLYDAK LDHQPVVAIV GQKARTSLGG NDQQEVDLMS
LFKDVASEYI QMATEPSQVR HLVDRAVRIA QAERTVTCVI VPNDLQELDY QEPKHEHQTI
HSGIGYLTPR VLPQDADLHR AAEVLNAGKK VAILIGVGAK NAAQEVIQLA DVLGAGVAKA
YLGKAVLPDE LPFVTGAIGL FGTNASHEMM QHCDTLFMIG SGFPYAEFLP KEGQARGVQI
DLDGRMLSIR YPMEVPLTGD SAETLRALLP LLQRKEDRSW REKIEENVKA WWQQVGEAAH
EEADPLNPRL VFEKLSPLLP DNVIMAADSG SSSSWMAQHI RIREGMQFSV SGTLATMGCA
VPYAIAAKFA HPDKLAIAFA GDGAMQMNGN EELITIQRYW RTWADPRLIV LVLNNKDLNF
VSWEQRLMQG EPKFHESQDL PDFKYAEYAE SLGLIGITID SPDQVEDAWK KALEAKRPVV
IEAITDPEVL VFNAKVAMKY APNLASAIVH GDTGAAEHLG DTLRAAVGL
//
