ID W2VKH5_9FIRM Unreviewed; 644 AA.
AC W2VKH5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Thiamine pyrophosphate enzyme, N-terminal TPP binding domain protein {ECO:0000313|EMBL:ETO98685.1};
GN ORFNames=HMPREF1495_0215 {ECO:0000313|EMBL:ETO98685.1};
OS Lachnoanaerobaculum sp. MSX33.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936596 {ECO:0000313|EMBL:ETO98685.1, ECO:0000313|Proteomes:UP000018910};
RN [1] {ECO:0000313|EMBL:ETO98685.1, ECO:0000313|Proteomes:UP000018910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSX33 {ECO:0000313|EMBL:ETO98685.1,
RC ECO:0000313|Proteomes:UP000018910};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (DEC-2013) 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:ETO98685.1}.
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; AZXX01000038; ETO98685.1; -; Genomic_DNA.
DR RefSeq; WP_034212195.1; NZ_AZXX01000038.1.
DR AlphaFoldDB; W2VKH5; -.
DR PATRIC; fig|936596.3.peg.724; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000018910; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..109
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 229..364
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 438..593
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 644 AA; 71394 MW; 044F8E1B2C0CD1C9 CRC64;
MKIKLSNYIA KRLVELGISH GFSVTGGGAM HLNDGLGHQE GLTITYNHHE QACAMAAEAY
ARINNQMAVL CVTTGPGGTN AITGVLGAWL DSIPMFVISG QVRYDWTARY SGTGIRAMGD
QEFDICKSIE CMSKYSEMIT EPMRIRYLVE KCAYLATHGR PGPVWLDIPL DVQGSIIEED
ELIGFDIGNY ESGGDGWAKP SPYKIDVDNR TKLDLGNEPK PLSRDVFIEI IDRIRKAKRP
VFNAGNGIRI GNAHKEFMEL AEILNIPVVV GWNSEDCIEV DHPLYAGRPG NFGDRPGNFT
VQNSDLLLSV GSRLSLRQVG FNYKGWAREA FTIVNDIDKE ELKKPTVHID IPVHADCKVF
MRQLIDVLKE QKTPVFEGGE GLKGMSWNET VKYWLKKYPV CRKEFLEKDD SKKANVYAFI
KEIGDRAKEN QITVVGNGSA CVVGGHSYII KKGQRFISNS AVASMGYDLP AAIGAYMANI
EGKRFDKELI LITGDGSIQM NLQELQTIVH HKADIKIFLI NNEGYHSIRQ TQNKFFGDKP
LVGIGPDSGD LSFPSMEKIA NAYGINYIGA KTNSEIADAV EKAFKAEGPV ICEAFVTTEQ
NFEPKSSGKQ MPDGRMVSPP LEDLVPFLSD EEMDENMIIP RMPE
//
