ID L0F594_DESDL Unreviewed; 548 AA.
AC L0F594;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:AGA68205.1};
GN OrderedLocusNames=Desdi_0676 {ECO:0000313|EMBL:AGA68205.1};
OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA68205.1, ECO:0000313|Proteomes:UP000010797};
RN [1] {ECO:0000313|Proteomes:UP000010797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Boon N., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP003344; AGA68205.1; -; Genomic_DNA.
DR RefSeq; WP_015261207.1; NC_019903.1.
DR AlphaFoldDB; L0F594; -.
DR STRING; 871963.Desdi_0676; -.
DR KEGG; ddl:Desdi_0676; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000010797; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Ligase {ECO:0000313|EMBL:AGA68205.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010797};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 548 AA; 58827 MW; 58314DD5C695E246 CRC64;
MEGKCRAGAL VSEVLKKEGA KYIFGIPGGH IYPAMERCEE LGIPFIGVRH EMTAAFAAEG
WALTTGKFGV CTGTAGPGVT NLLTGLANSY VGGFPVFALG GKARVTENDR NELQDFNQMA
ILSQMTKHAR AVSEPKRIPE YVGRAIAHAT TGKPGPVYIE VPRDLMETEV DLSTVEFQER
YITESKPQGD PASIQAALEL IKEAQKPVII AGSGVWFSQA HHELQAFVEK TGIPFATRNA
ARGCITDKHP LFISPGYDHP ILQALLAEAD LAIVIGTRPG FTLGRGNFRK DMKIIRIDID
AAELNNQLDV KVGIHGDAKE VLKQLNAGVE SASRPQWVGF LNAVKQQFAG LFGQMCDPSH
SPIHPVHLMS QIAQRVNEET IVVVDGGDTA TWATLALPAY GPGQMLSIAA TSFGPLGVGM
GYAIAAKLAH PEKKVIMITG DGAFGYGVAE FDTLKRYGLD ITTIILNDGL WGMIKRSEAK
KANGKAKFVG VELMEQVHYE KVVESLGGYG EFVTDPAEVG NAIDRALACG KMSCVNVITD
PQFGPPSR
//
