ID A0A0E8U3K5_MYCTX Unreviewed; 582 AA.
AC A0A0E8U3K5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:CFH71927.1, ECO:0000313|EMBL:SGH06810.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:CFH71927.1, ECO:0000313|EMBL:SGH06810.1};
GN Name=oxc {ECO:0000313|EMBL:SGH06810.1};
GN ORFNames=A4S10_00132 {ECO:0000313|EMBL:OMH57984.1}, ERS053720_00690
GN {ECO:0000313|EMBL:CFH71927.1}, SAMEA2683035_00267
GN {ECO:0000313|EMBL:SGH06810.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:SGH06810.1, ECO:0000313|Proteomes:UP000182946};
RN [1] {ECO:0000313|EMBL:CFH71927.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH71927.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OMH57984.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH57984.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SGH06810.1, ECO:0000313|Proteomes:UP000182946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGH06810.1,
RC ECO:0000313|Proteomes:UP000182946};
RG Pathogen Informatics;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH57984.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH57984.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-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}.
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DR EMBL; CFSW01000003; CFH71927.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH57984.1; -; Genomic_DNA.
DR EMBL; FPTZ01000001; SGH06810.1; -; Genomic_DNA.
DR RefSeq; WP_003900812.1; NZ_WCJH01000003.1.
DR AlphaFoldDB; A0A0E8U3K5; -.
DR PATRIC; fig|1773.211.peg.1906; -.
DR OMA; MRVISFR; -.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; 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:SGH06810.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 408..552
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 61171 MW; E9F571E02755292E CRC64;
MTTRSASPCT VLTDGCHLVV DALKANDVDT IYGVVGIPIT DLARAAQASG IRYIGFRHEA
SAGNAAAAAG FLTARPGVCL TTSGPGFLNG LPALANATTN CFPMIQISGS SSRPMVDLQR
GDYQDLDQLN AARPFVKAAY RIGQVQDIGR GVARAIRTAT SGRPGGVYLD IPGDVLGQAV
EASAASGAIW RPVDPAPRLL PAPEAIDRAL DVLAQAQRPL LVLSKGAAYA QADNVIREFV
EHTGIPFLPM SMAKGLLPDS HPQSAAAARS LAMARADVVL LVGARLNWLL GNGESPQWSA
DAKFIQVDIE ASEFDSNRPI VAPLTGDIGS VMSALLEAAA DRSSVASAAW TGELADRKAR
NSAKMRRRLA DDHHPMRFYN ALGAIRSVLQ RNPDVYVVNE GANALDLARN IIDMHLPRHR
LDSGTWGVMG IGMGYAIAAA VETGRPVVAI EGDSAFGFSG MEFETICRYR LPVTVVILNN
GGVYRGDEAT IFRSAAPVWR HDPAPTVLNA HARHELIAEA FGGKGYHVST PTELESALTD
ALASNGPSLI DCELDPADGV ESGHLAKLNT TSAATPAISG DG
//
