ID A0A158M1Z9_9BORD Unreviewed; 554 AA.
AC A0A158M1Z9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Thiamine pyrophosphate enzyme, N-terminal TPP binding domain protein {ECO:0000313|EMBL:KAK87278.1};
GN ORFNames=L497_0886 {ECO:0000313|EMBL:KAK87278.1};
OS Bordetella holmesii CDC-H585-BH.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK87278.1, ECO:0000313|Proteomes:UP000026682};
RN [1] {ECO:0000313|EMBL:KAK87278.1, ECO:0000313|Proteomes:UP000026682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK87278.1,
RC ECO:0000313|Proteomes:UP000026682};
RA Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA Losada L.;
RT "Genome sequence of Bordetella holmseii.";
RL Submitted (MAR-2014) 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:KAK87278.1}.
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DR EMBL; JFZZ01000137; KAK87278.1; -; Genomic_DNA.
DR RefSeq; WP_005013479.1; NZ_JFZZ01000137.1.
DR AlphaFoldDB; A0A158M1Z9; -.
DR STRING; 35814.BBB42_07700; -.
DR GeneID; 56625225; -.
DR PATRIC; fig|1331206.3.peg.3327; -.
DR Proteomes; UP000026682; 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; 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 2..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 554 AA; 59823 MW; 32E43121C479C949 CRC64;
MGGHILVDQL FAHGVKHVFC VPGESYLAVL DGLHDASIEV TVCRQEGGAA MMADAHGKLT
GEPGICMVTR GPGAANALAG IHIAKQDSSP LILFVGQIER GMREREAFQE MDYRAVFGTQ
AKWVTEIDQV ERIPELISRA FHVATSGRPG PVVIALPEDM LVEMADVPDA PHYEVIDAAP
ASDQMDTLTQ MLASARKPVA ILGGTRWDAQ AVAQFADFAR AHALPVGVSF RRQMLFPADH
PCYVGDVGLG INPALLARVR EADLILLVGG RMSENPSQAY TLLDIPVPRQ KLVHVHPDSA
ELARVYRPNL AVNVSPTAFC AALASIPAPE AAPSWAADTE RMRQNYLAWS DPSQIKTPGS
LQMGEVMAYL EDALPPDAIM TNGAGNYASW LHRFHRHTRY ATQLAPTSGS MGYGLPAAVG
AKRIWPDKTV ICFAGDGCFL MHGQEFATAV QYDLPIIVVL VDNGMYGTIR MHQEKHYPGR
VSATQLKNPD FADYARAFGG HGERVETSAE FGPAFERARA SGKPAILHCL IDPETISPST
TLEKIRAAAL EAKA
//
