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Database: UniProt
Entry: A0A177R122_9PROT
LinkDB: A0A177R122_9PROT
Original site: A0A177R122_9PROT 
ID   A0A177R122_9PROT        Unreviewed;       560 AA.
AC   A0A177R122;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:OAI52846.1};
GN   ORFNames=AYO46_04150 {ECO:0000313|EMBL:OAI52846.1};
OS   Betaproteobacteria bacterium SCGC AG-212-J23.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1799662 {ECO:0000313|EMBL:OAI52846.1, ECO:0000313|Proteomes:UP000077532};
RN   [1] {ECO:0000313|Proteomes:UP000077532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-J23 {ECO:0000313|Proteomes:UP000077532};
RA   Choi J., Stepanauskas R., Howe A.;
RL   Submitted (FEB-2016) 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:OAI52846.1}.
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DR   EMBL; LSTF01000030; OAI52846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177R122; -.
DR   Proteomes; UP000077532; 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   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077532};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..124
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..333
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          389..534
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   560 AA;  60734 MW;  A843B74D22022980 CRC64;
     MKSDLKTRHG GKILADALVA QGVKLAFGVP GESYLPVLDG MYDTRERLSF VICRQEGGAS
     YMAEAYGKLT GEPGVLFVTR GPGATNGAIG VHTGLQDSTP MVVFIGQVPN EFAEREAFQE
     IDYRRMYGQM AKWVGQIDRV ERIPEYVSHA FHTACAGRPG PVVLALPEDA LYGQAAVADV
     PRYHKVRPAP SPQGISELNG LLQKAEKPFV LIGGGGWDRE ACLKLQKWVE ANGLAAGTSF
     RCQDLFDNRS PNYAGDVGIG INPKLAERVK EADVLLVIGA RLGEMTTGAY SLVEAPLPRQ
     TLVHVHGGAE ELGRVYRPSL AINSGMAQFV DALSPLSFSK PGWKADTEAL RKDYLQWTEP
     RPMPGKLQYG EVIRWLSDNL PQDAIVAGGA GNFAGWLHRH FRYKGFRTQL GSTNGSMGYG
     YPAAVAAKLA EPKRTVLGLC GDGDFLMTGQ EIATAAQYGA NFVALVVNNG IYGTIRMHQE
     REYPGRVFGT DLKNPDFAAY ARAFGGHGET VERTEDFAPA FERASRSGKP ALIELKIDPD
     AITPTMTLSA IREKALTSKR
//
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