ID I2AL03_9MYCO Unreviewed; 578 AA.
AC I2AL03;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Putative oxalyl-CoA decarboxylase {ECO:0000313|EMBL:AFJ37977.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:AFJ37977.1};
GN ORFNames=W7S_25140 {ECO:0000313|EMBL:AFJ37977.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ37977.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ37977.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ37977.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(2012).
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; CP003491; AFJ37977.1; -; Genomic_DNA.
DR RefSeq; WP_014712551.1; NC_017904.1.
DR AlphaFoldDB; I2AL03; -.
DR KEGG; mmm:W7S_25140; -.
DR PATRIC; fig|1168287.3.peg.5111; -.
DR HOGENOM; CLU_013748_3_3_11; -.
DR Proteomes; UP000002868; 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:AFJ37977.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..134
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 413..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 578 AA; 60444 MW; 8B7A1A3250878185 CRC64;
MSTVSASGSD AQGSTRVIDG FHLVVEALRA NDVATIYGLV GIPITDLART AQAAGIRYIG
FRQEASAGNA AAAAGFLTRR PGVCLTTSGP GFLNALPALA NATTNCFPMI QISGSSNRAL
VDLQRGDYQD LDQLNAARPF AKAAFRVNRI EDIGRGVARA IRTAVSGRPG GVYLDIPGDV
LGQALEASAA AGTIWRVVDP APRQLPAPDA VDRALEVLAR ARRPLIVLGK GAAYAQADNE
IRRFVEATGI PFLPMSMAKG LLPDSHPQSA ATARSLAISR ADAVLLIGAR LNWLLGHGES
PQWSSDTKFV QVDIAASEFD SNQPIAAPLA GDIGSVMSAL CDAVTARPFA APTKWATELA
DRKARNDAKM RERLADDPHP MRFYNALGAI RAVLQDNRDV YIVNEGANAL DLARNVIDME
LPRHRLDTGT WGVMGIGMGY AIAAAVETGG PVVAIEGDSA FGFSGMEIET ICRYRLPVTV
VILNNGGVYR GDETAAHPSD PAPTVLNARA RHELIAEAFG GKGYHVTTPD ELRAALTEAI
SSGAPSVIDC ELDPAAGVES GHLAGLNPAR AAAVSGGG
//
