ID C4GCK6_9FIRM Unreviewed; 618 AA.
AC C4GCK6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Thiamine pyrophosphate enzyme, central domain protein {ECO:0000313|EMBL:EEP27706.1};
GN ORFNames=GCWU000342_01700 {ECO:0000313|EMBL:EEP27706.1};
OS Shuttleworthia satelles DSM 14600.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Shuttleworthia.
OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP27706.1, ECO:0000313|Proteomes:UP000003494};
RN [1] {ECO:0000313|EMBL:EEP27706.1, ECO:0000313|Proteomes:UP000003494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP27706.1,
RC ECO:0000313|Proteomes:UP000003494};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP27706.1}.
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DR EMBL; ACIP02000004; EEP27706.1; -; Genomic_DNA.
DR RefSeq; WP_006906695.1; NZ_GG665867.1.
DR AlphaFoldDB; C4GCK6; -.
DR STRING; 626523.GCWU000342_01700; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_3_9; -.
DR Proteomes; UP000003494; 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 Reference proteome {ECO:0000313|Proteomes:UP000003494};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 213..349
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 417..568
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 618 AA; 68367 MW; 0C356B317FAE4ED5 CRC64;
MKQRLADYVA DYLVNWGIRN CFTVTGGGAM HLNDAFGHHP GLKSIYNHNE QGSAIAAEAY
ARWNNRPALL CVTTGPGGTN AITGVVGGWL DSIPMLIISG QVRYDTTARY NEQFTQGYHL
RAVGDQEYDI TKSVSNMCKF AKMIEDPRTI RHDLERALHL ATTGRPGPVW LDIPVNYQGG
IIETDDLVAY SPEEMAEDDA AQNLPSPVSA ETVQTVLDKV RAAKRPVLYA GNGIRLSGGY
DAFREAVEKL GIPVVTYWDA IDLIETDHPL YCGRGGNMGD RAGNFAVQNA DLVLAVGNRL
PIRVVGYNWK TWAREAEVIM VDVDPAELRK PTIHVEMPIH ADAGDFFERV NALCEGNDKL
VSAASDWRQI CENWKKDYPV VLPRHREEND RFANAYAAFD SISSRLPEGT LVITSNGTCC
VAGHQSWVIK KGTRFFNNNA IASMGYGLPA AIGGCMAHDQ KMTICLEGDG SIMMNLQELQ
TISTNHLPIK IVLINNQGYH SIRQTQNNLF GGRPKVGIGP ESHDLSFPEY RKIAAAFDIP
YVEAHSNAQL AEGYEKMMAT DGPVLFEIFV STEQIFEPKS STKRLEDGTL VSPPLEDLAP
FLPREEFLKN MYIKPVEE
//
