ID A0A254Q050_9BURK Unreviewed; 568 AA.
AC A0A254Q050;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:OWS72189.1};
GN ORFNames=CBI30_03070 {ECO:0000313|EMBL:OWS72189.1};
OS Polynucleobacter aenigmaticus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1743164 {ECO:0000313|EMBL:OWS72189.1, ECO:0000313|Proteomes:UP000198104};
RN [1] {ECO:0000313|EMBL:OWS72189.1, ECO:0000313|Proteomes:UP000198104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-K35W1 {ECO:0000313|EMBL:OWS72189.1,
RC ECO:0000313|Proteomes:UP000198104};
RA Hahn M.W.;
RT "Polynucleobacter sp. MWH-K35W1 isolated from the permanently anoxic
RT monimolimnion of a meromictic lake.";
RL Submitted (MAY-2017) 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}.
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:OWS72189.1}.
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; NGUO01000004; OWS72189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254Q050; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000198104; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008949; F:oxalyl-CoA decarboxylase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0033611; P:oxalate catabolic process; 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; IPR045025; HACL1-like.
DR InterPro; IPR017660; Oxalyl-CoA_decarboxylase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR03254; oxalate_oxc; 1.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 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 13..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 568 AA; 60432 MW; A054E7DCBF26F16F CRC64;
MTTDNQNTQV TDGFHLVIDA LKANDLDTIF GLVGIPITDL CRLAQAEGLR FIGFRHEQHA
GNAAAIAGYM TQKPGICMTV SAPGFLNGLT ALANATVNCF PMILISGSSE REIVDLQQGD
YEEMDQLNAA KPYCKAAYRI NHIEDIGIGF ARAIRAAVSG RPGGVYLDLP AKLLAQTMPV
EEAKKSIFKV IDPIPRQIPA PDAVERALNV LKGAKRPLIL LGKGAAYAQA DADIRALIEK
SGIPYLPMSM AKGLLPDNHP QSASAARSFV LAEADAVLLV GARLNWLLAH GKGKTWGKDP
KKFIQIDIQA NEVDSNVQID APLIGDIGSC VGELLKGIAA VPKPAAEWIA AINEKKDKNL
AKMAETLAKD ASPMNFHGAL RAIRDVIKLN PDVNLVNEGA NTLDYCRAIV DMYKPRKRFD
SGTWGIMGIG MGYAIGAAVT SGLPTVAVEG DSAFGFSGME LETICRYNLP ITTVVFNNNG
VYRGTDVNPT GGADVAPTVF VKNARYDKMI EAFGGVGYYV TTPAELEAAL TKAIAEGKPA
LINAVIDETA GTESGRLTNL NPSTAGKK
//
