ID A0A2G2JZG2_9PROT Unreviewed; 261 AA.
AC A0A2G2JZG2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Thiamine pyrophosphate enzyme N-terminal TPP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COA89_16510 {ECO:0000313|EMBL:PHS03721.1};
OS Acidithiobacillus sp.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1872118 {ECO:0000313|EMBL:PHS03721.1, ECO:0000313|Proteomes:UP000221235};
RN [1] {ECO:0000313|Proteomes:UP000221235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:PHS03721.1}.
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DR EMBL; NVVQ01000085; PHS03721.1; -; Genomic_DNA.
DR Proteomes; UP000221235; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
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; IPR045229; TPP_enz.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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); 1.
PE 3: Inferred from homology;
FT DOMAIN 1..104
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 185..251
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
SQ SEQUENCE 261 AA; 27889 MW; 87FDB9B2C9482B2E CRC64;
MDCNDLIAQI LXKXGVEWLA CFPSNPLIEA VAKQGIRPIS FRHERGAVMX ADGFSRTSDR
KRFGVVAIQS QAGAENALGG VAQAYADNIP ILILPGGVGL SELAVRPNYS VTNNYQGVVK
RVEAIYRPDQ VIAVMRRAFS ALRNGAPGPV AVELIADVCE TTATENIXQY IPPRXVKQQP
DSSDIKAAVQ IFLGARRPML WAGAGVLFAG AMSELKNLAE LTATPVFTTM PGKSGFDERH
PLALGAGCGL RYNNRASPTV A
//
