ID A0R305_MYCS2 Unreviewed; 576 AA.
AC A0R305;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:ABK75186.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:ABK75186.1};
GN OrderedLocusNames=MSMEG_5297 {ECO:0000313|EMBL:ABK75186.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK75186.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK75186.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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; CP000480; ABK75186.1; -; Genomic_DNA.
DR RefSeq; YP_889543.1; NC_008596.1.
DR AlphaFoldDB; A0R305; -.
DR STRING; 246196.MSMEG_5297; -.
DR PaxDb; 246196-MSMEI_5154; -.
DR KEGG; msm:MSMEG_5297; -.
DR PATRIC; fig|246196.19.peg.5167; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000000757; Chromosome.
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:ABK75186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 211..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 411..548
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 576 AA; 60161 MW; 21846F27D9EAE450 CRC64;
MNTAPLMTES VPGTSPVTDG AHVLVDALKL NGVETLYGVV GIPITDVARV AQAQGLRYIG
FRHESDAGHA AAAAGFLTKK PGFCLTVSAP GFLNGLVALA NATTNCFPMV QISGSSDRHI
VDLQRGDYEE MDQLAAAKPF VKAAFRVNRA ADIGLAVARA IRTASSGRPG GVYLDIPAAV
LGEVIDAGAA AASLRTVVDA APEQLPPPRA VDRAVALLAA ARRPLVVLGK GAAYAQADKT
IRNFLESTGL PFLPMSMAKG LLPDTHPQSV ASARSMALRD ADVVLLVGAR LNWLLGHGEP
PQFSRDVKFI QVDIDPGELD SNAPIAAPLV GDIGSVIEAL AERAQFIDAP APWREQLAER
KARNAESMAK RLAADPRPMR FHGALRAIRD VLRDRPDVYV VNEGANALDL ARNVIDMAVP
RHRLDSGTWG VMGVGMGYAI AAAVEGSGPV VAIEGDSAFG FSAMELETIC RYRLPVVVVV
LNNGGVYRGD GHNPASDDPS PTTLMPAARH DRLIEAFGGT GHHVTTPAEL GAALTEALAS
GGPALIDCVI DPADGTESGH LTQLNPAVVG HHPATN
//
