ID A0A3N6Q558_9BURK Unreviewed; 582 AA.
AC A0A3N6Q558;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:RQH07506.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:RQH07506.1};
GN ORFNames=D1Y85_08995 {ECO:0000313|EMBL:RQH07506.1};
OS Paraburkholderia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2305225 {ECO:0000313|EMBL:RQH07506.1, ECO:0000313|Proteomes:UP000272778};
RN [1] {ECO:0000313|EMBL:RQH07506.1, ECO:0000313|Proteomes:UP000272778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOA04 {ECO:0000313|EMBL:RQH07506.1,
RC ECO:0000313|Proteomes:UP000272778};
RA Gao Z.-H., Qiu L.-H., Fu J.-C.;
RT "Paraburkholderia sp. DHOA04, isolated from soil.";
RL Submitted (NOV-2018) 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:RQH07506.1}.
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DR EMBL; RQIS01000005; RQH07506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6Q558; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000272778; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008949; F:oxalyl-CoA decarboxylase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:RQH07506.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272778};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 23..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 214..346
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 418..556
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 61432 MW; F3EA40F31AE0F823 CRC64;
MAEAGINEAQ NSPAPEAQQT TDGFHLVIDA LKLNDIDTIF GLVGIPITDL ARLAQAEGMR
FIGFRHEQNA GNAAAVAGYM TKKPGVCLTV SAPGFLNGLT ALANATTNCF PMILISGSSE
REIVDLQQGD YEEMDQLNAA KPYAKAAYRV LHAEDIGIGV ARAIRAAVSG RPGGVYLDLP
AKLLAQTMDA VKGKQSLVKV VDAAPRQIPA PESVKRALDV LKGAKRPLIL LGKGAAYAQA
DAQIRALVEK TGIPYLPMSM AKGLLPDTHE QSASAARSFV LAEADVVMLV GARLNWLLSH
GKGKTWGAES GPKQFIQIDI APTEIDSNVA IEAPVIGDIG SCVEALLEGV GDNFPQPGAE
WLNAIAERKN KNLAKMAATL EKNPSPMNFH SALRAIRDVL KTRPDINVVN EGANTLDYAR
SIIDMYQPRK RFDSGTWGIM GIGMGFAVGA AVTSGTQVVA IEGDSAFGFS GMELETICRY
NLPVCTIVFN NNGVYKGTDV NASGGADMAP TAFVKNARYD KMMEAFGGVG HNATTPEELT
AALLEAIASG KPTVINAVID ESAGTESGRL TNLNPQSAAM KK
//
