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Database: UniProt
Entry: K2KQ61_HELPX
LinkDB: K2KQ61_HELPX
Original site: K2KQ61_HELPX 
ID   K2KQ61_HELPX            Unreviewed;       314 AA.
AC   K2KQ61;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Thiamine pyrophosphate enzyme, C-terminal TPP binding domain protein {ECO:0000313|EMBL:EKE84609.1};
GN   ORFNames=OUG_1102 {ECO:0000313|EMBL:EKE84609.1};
OS   Helicobacter pylori R32b.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1145112 {ECO:0000313|EMBL:EKE84609.1, ECO:0000313|Proteomes:UP000006767};
RN   [1] {ECO:0000313|EMBL:EKE84609.1, ECO:0000313|Proteomes:UP000006767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R32b {ECO:0000313|EMBL:EKE84609.1,
RC   ECO:0000313|Proteomes:UP000006767};
RX   PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA   Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA   Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA   Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT   "Genome sequences of 65 Helicobacter pylori strains isolated from
RT   asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT   disease, or gastritis.";
RL   Pathog. Dis. 68:39-43(2013).
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:EKE84609.1}.
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DR   EMBL; AMOS01000003; EKE84609.1; -; Genomic_DNA.
DR   RefSeq; WP_000589025.1; NZ_AMOS01000003.1.
DR   AlphaFoldDB; K2KQ61; -.
DR   PATRIC; fig|1145112.3.peg.1086; -.
DR   Proteomes; UP000006767; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03376; TPP_PFOR_porB_like; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          51..218
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          147..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   314 AA;  34998 MW;  37E9941F7A4974A7 CRC64;
     MIKEVKTLKG FSQSAEKFQG SHLLCPGCGH GIIVREVLNA VDGPIVLGNS TGCLEVCSAV
     YPHTSWDVPW IHIGFENGST AISGVEAMYK ALTNKGRYQG QKPKFVAFGG DGASYDIGLQ
     FISGCMERGH DMTYICLDNE NYANTGGQRS GSTPLGASTS TTPAGSVSFG KKEKKKDIVN
     IMASHGVPYV AQLSPNKWKD MNKKIKTALD TEGPCFINAL SPCTTEWKFE SNKTIELADM
     AVDSLMFPLF EIFNGRELKI TYRPRNIIPV RDYLGAQKRF RHLFKKENEH IIEELQKDVN
     ERWEYLQRRE EAKV
//
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