ID A0A0S8CUF9_9PROT Unreviewed; 562 AA.
AC A0A0S8CUF9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KPK26701.1};
GN ORFNames=AMJ66_11640 {ECO:0000313|EMBL:KPK26701.1};
OS Betaproteobacteria bacterium SG8_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK26701.1, ECO:0000313|Proteomes:UP000051602};
RN [1] {ECO:0000313|EMBL:KPK26701.1, ECO:0000313|Proteomes:UP000051602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK26701.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK26701.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJTS01000241; KPK26701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CUF9; -.
DR PATRIC; fig|1703389.3.peg.1480; -.
DR Proteomes; UP000051602; 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 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
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..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 61143 MW; 5A5F23C3588E0B6C CRC64;
MNQDLSLRSG GQVLVDQLRI HGVDTAFCVP GESYLDVIDA LYDHRNAIRL IVSRQDGGAS
FMAEAYGKCT GKPGICLVTR GPGATNASIG VHTAYQDSTP MILFVGQVGG DVVEREAFQE
IDYRRMFGQM AKWVAQIDRA ERIPEYVSHA FHLAVSGRPG PVVLALPEDM LVTKVEVADA
RPFATNRAAP FSGAMDRVRD MLEEARQPLV LLGGGGWTPQ ACDDIRGFVE ANNLPVACTF
RRQDLIDNRH PNYCGDVGIG INPLLAKRVG AADLVIAVGP RLGEMTTNTY TLFDIPGPVQ
KMIHVHPGAE ELGRVYQADL MINSDMGEFA QLATRMPPVD SAPWRDWTHQ AHKDYLANIE
PQASPGAVDM AEVMTEMRKQ LPADAIMTNG AGNYSGWVQR YWQYGGLRTQ VAPTNGAMGY
GVPAGVAAKV ACPDRTVVSF SGDGCFLMNG QEIATAVQYD LKVLFVVINN GMYGTIRMHQ
ERDYPNRVHG TALRNPDFAA LARAYGMHGA VVRRTEEFAG VLAEALAQKT SALIEIQIDP
EAITTRGKLT AIRENALKRK GG
//
