ID A0A1W6ZJI2_9BORD Unreviewed; 562 AA.
AC A0A1W6ZJI2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:ARP97583.1};
GN ORFNames=CAL15_21360 {ECO:0000313|EMBL:ARP97583.1};
OS Bordetella genomosp. 13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463040 {ECO:0000313|EMBL:ARP97583.1, ECO:0000313|Proteomes:UP000194161};
RN [1] {ECO:0000313|EMBL:ARP97583.1, ECO:0000313|Proteomes:UP000194161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU7206 {ECO:0000313|EMBL:ARP97583.1,
RC ECO:0000313|Proteomes:UP000194161};
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}.
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DR EMBL; CP021111; ARP97583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6ZJI2; -.
DR STRING; 463040.CAL15_21360; -.
DR KEGG; bgm:CAL15_21360; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000194161; Chromosome.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 61318 MW; D3EB912218BAD0D3 CRC64;
MSDHSKLRTG GQLIAEALLA QRVDTVFCVP GESYLDVLNA LYAHQDAIRV VTCRHEGAAS
FMAEAHGKLS GRPGVCLVTR GPGATNASIG VHTAFQDSTP MVLLVGQVGR DMMEREAFQE
IDYRRMFGQF AKWAAQIDDA ARIPEFLARA FSVAQSGRPG PVVLALPEDM LTESAFPVET
AQVSVPQAHP APDAMQRMHE CLAHAQRPLL LLGGVGWEAD GREAITRFAQ QNGLPVACTF
RRQDLFDNRH PNYVGEVGIG LNPALAKAVR ESDLLIAVGT RLGEIVTSGY TLLDVPAPRQ
RLVHVLAAPE ELGRVYQATV PVLSHMNPFA RAAAALEPAA YSAARADWLQ TLRASYESYV
EPPLREARVD PAQVIVALRD TLQRDAILTN GAGNYSAWAH RYYPFSHARS QLAPTSGAMG
YGVPAAIAAK LRHPERQVVC LAGDGCFMMT AQELATVKRY GLDIVFIVFN NGMYGTIRMH
QETNYPGRPI GTDLCNPDFV MYAQSFGLRA ERVSRSQDFA PVLQRALQTG GAALIELEIE
PEILTPRATL TELRERALRQ TA
//
