ID E4PFG8_MARAH Unreviewed; 552 AA.
AC E4PFG8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Protein containing thiamine pyrophosphate enzyme, C-terminal TPP-binding / Thiamine pyrophosphate enzyme, N-terminal TPP binding region {ECO:0000313|EMBL:ADP96717.1};
GN OrderedLocusNames=HP15_953 {ECO:0000313|EMBL:ADP96717.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP96717.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP96717.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CP001978; ADP96717.1; -; Genomic_DNA.
DR RefSeq; WP_014576432.1; NC_017506.1.
DR AlphaFoldDB; E4PFG8; -.
DR STRING; 225937.HP15_953; -.
DR GeneID; 78559556; -.
DR KEGG; mad:HP15_953; -.
DR PATRIC; fig|225937.3.peg.964; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_8_0_6; -.
DR OMA; CGVEVCF; -.
DR Proteomes; UP000007077; Chromosome.
DR GO; GO:0003824; F:catalytic activity; 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; 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.
PE 3: Inferred from homology;
FT DOMAIN 3..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 371..513
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 319..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 58116 MW; A6CB032F64A2074E CRC64;
MTNGAQALMK TLVDAGVEVC FSNPGTSEMH FVAALDDEPK MRAVLALFEG VATGAADGYA
RMADKPAATL LHLGCGLGNG LANLHNARKG KVPVLNIVGD HATYHVKYDA QLQSDIETVA
RNVSPGFVRT AKSTETLCQD AAEAIAAART APGQVATLIL PADVSWGEGG VPSAPLAPPT
PEPADDATVE AIAKAIRSGK KTALLMGGHS LREPSMLAAA KLAAHSGVTL LAETFPTRME
RGAGLPYIER IAYLAELATV QLTDIEQLIL VDSKAPVSFF AYPGKKSYLV PDTCQVHTLA
APDQDILASL NKLNDAVGAS QAQPKLQPEK RPGRPRGKLT AEKVCKAVGE LMPENAIIVD
EGITSSLMLS VMTAGAPRHD MITLTGGAIG QGLPNAVGAA VACPDRPVIA LIGDGTAMYT
IQALWTMARE QLNVTSIIFN NASYSVLNIE LERVGAEEAG EKAKSQLDLR GPVINFAEMA
NGMGVHGVRV HTAEEMAKAL EYAQRMPGPH VIEAMIPESL SGVKRRVLPW MLRALPSLPV
SVSRALKRKL AP
//