ID A0A1A0NVC5_9MYCO Unreviewed; 599 AA.
AC A0A1A0NVC5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Thiamine pyrophosphate-requiring protein {ECO:0000313|EMBL:OBB01332.1};
GN ORFNames=A5662_13770 {ECO:0000313|EMBL:OBB01332.1};
OS Mycobacteriaceae bacterium 1482268.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae.
OX NCBI_TaxID=1834080 {ECO:0000313|EMBL:OBB01332.1, ECO:0000313|Proteomes:UP000091934};
RN [1] {ECO:0000313|EMBL:OBB01332.1, ECO:0000313|Proteomes:UP000091934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1482268.1 {ECO:0000313|EMBL:OBB01332.1,
RC ECO:0000313|Proteomes:UP000091934};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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:OBB01332.1}.
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; LZSH01000207; OBB01332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A0NVC5; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000091934; 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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 599 AA; 64281 MW; 8D8E568B5946BC12 CRC64;
MGQQVADFVL DRLRQWGVRQ VFAYPGDGIN GLVAAFGRAD NQPQFVQARH EEMAAFSATG
YAKFSGEVGV CMATSGPGAI HLLNGLYDAK LDHVPVVAIV GQTERSAMGG SYQQEVDLQA
LFRDVASDYL VEVNVPEQLP LAIDRAIRTA CARRSPTAVI IPSDLQEEKY SPPAHVFKQV
PSSAPGDDVG LLTPTDEQAR AAADILNAGE KVAILIGQGA RGAADEVVAV AELTGAGVAK
ALLGKDVLPD DLPYVTGSIG LLGTRPSYEM MRDCDTLLIV GSNFPYSQFL PDYGAARAVQ
IDVDGSGIGM RYPTELNIVA DAKAALAALI PHLRPKADSS WRAGVERNVA RWWEVLERQS
MLTAKPVNPM RVAWELSERL PDGAIVTADS GSSTNWFARC VKLRAGMRAS VSGTLATMGC
AVPYAIGAKF AHPARPVIAL VGDGAMQMNG LAELLTIRRY REQWADQRLV ICVFHNNDLN
QVTWELRAMG GAPKFEESQS LPEVSYAEVA RTMGLRAIAV DSDDAVAGAW DEALSYDEPV
VLDVTCDPEV PPIPPHATYE QVKELTSAVL GGDPAAWHLM YQGAKTKFQE LVPGSRSDG
//
