ID A0A261SB31_9BORD Unreviewed; 596 AA.
AC A0A261SB31;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Thiamine pyrophosphate-requiring protein {ECO:0000313|EMBL:OZI34599.1};
GN ORFNames=CAL29_13980 {ECO:0000313|EMBL:OZI34599.1};
OS Bordetella genomosp. 10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416804 {ECO:0000313|EMBL:OZI34599.1, ECO:0000313|Proteomes:UP000216020};
RN [1] {ECO:0000313|EMBL:OZI34599.1, ECO:0000313|Proteomes:UP000216020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU16122 {ECO:0000313|EMBL:OZI34599.1,
RC ECO:0000313|Proteomes:UP000216020};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-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:OZI34599.1}.
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DR EMBL; NEVM01000002; OZI34599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261SB31; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000216020; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 596 AA; 64249 MW; C0AF35D718C8B0E8 CRC64;
MATTVGDFLV DRLYAWGVRR IFGYPGDGIN GVFGALRRAR GKIEFVQARH EEMAAFMASA
HAKFTGELGV CIATSGPGAS HLLTGLYDAR MDHVPVLAIA GQQARASLGG HYQQELDLVS
MFKDVAGAFV QQAVVPGQVR HLVDRAVRTA LAERKVTALV LPNDLQELGY EPPGHKHGTV
HSGVGYQAPR LLPFKEDLER AAEVLNAGKK VAILVGAGAL AATDEVIAVA DRLGAGVAKA
LLGKAVLPDD TPWVTGSIGL LGTKPSYEMM EACDTLLMIG SGFPYSEFLP KEGAARGVQI
DIKADMLSLR YPMEVSLVGD SAQTLRELLP LLEQKTDTRW RDDIAHWTGR WWKTLEKRAL
EPGREGVNPQ RSVWELSSRV PADAVVTSDS GSVANWYARD LKVQRGMMCS LSGGLASMGA
AVPYAIAAKF AHPARPVIAL VGDGAMQMNN MAELITVAKY WEQWADPRWI CMVLNNGDLN
QVTWEQRVMN GDPKFSASQD IPSIPYHAFA EMIGLKGIYV DQDDMLGAAW DTALHADRPV
VIEVKADPSV PPLPPHITMT QARAFGKALL QGDPDQGNVV IDTARQVLGS VLPGGA
//
