ID C6XPM0_HIRBI Unreviewed; 514 AA.
AC C6XPM0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ACT60285.1};
GN OrderedLocusNames=Hbal_2610 {ECO:0000313|EMBL:ACT60285.1};
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT60285.1, ECO:0000313|Proteomes:UP000002745};
RN [1] {ECO:0000313|Proteomes:UP000002745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC {ECO:0000313|Proteomes:UP000002745};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CP001678; ACT60285.1; -; Genomic_DNA.
DR RefSeq; WP_015828435.1; NC_012982.1.
DR AlphaFoldDB; C6XPM0; -.
DR STRING; 582402.Hbal_2610; -.
DR KEGG; hba:Hbal_2610; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_8_0_5; -.
DR OMA; DFRHEEP; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000002745; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
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:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 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:UP000002745}.
FT DOMAIN 1..105
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 375..512
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 514 AA; 54839 MW; 5A16C910B621AB3D CRC64;
MNGAESLVST LIDQNVDICF ANPGTSEMHF LAALDNPKMK SVLCLFEGVA TGAADGWYRM
KETPASTLLH LGPGLANGLA NIHNAKRASS GMVNIVGEHS MSHLKYDPPL ASDIEGLARP
LSHWVRRADS ASSIAWDTAS AVAAANAHPG QISTLILPGN TSWEEAAPTH ALPQVKHEKR
VPDTGRIENV ANILKSGEPA LIVLANKATK GRALELAGKV SASCKCRLGT QFFTARIERG
AGRVPLERIP YAVPQAIEFL KGFKHIITVE TNEPTAFFSY PDKPSLLKDP STNVHCLVEK
DEDSELAFEM LLEAIGGQDA APILQERVET PAPTGELIPL SIAHALAHSI PENAIVIDES
LTTGRETMGH TVGARPHDLI NNLGGSIGYA TPLSIGAALA CPDRRVVCMV GDGSAMYTIQ
SLWTQAREGL NITTIIFANN KYAILKAEYA NMGAGTPGEQ AMAMIDIDRP TINWVSMANS
MGVSARSVNT AEDFTKAMLD SFNEPGPSLI EVQL
//