ID   A0A0A7IC61_9BIFI        Unreviewed;       590 AA.
AC   A0A0A7IC61;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:AIZ16815.1};
DE            EC=4.1.1.8 {ECO:0000313|EMBL:AIZ16815.1};
GN   ORFNames=AH67_07820 {ECO:0000313|EMBL:AIZ16815.1};
OS   Bifidobacterium pseudolongum PV8-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ16815.1, ECO:0000313|Proteomes:UP000030636};
RN   [1] {ECO:0000313|EMBL:AIZ16815.1, ECO:0000313|Proteomes:UP000030636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ16815.1,
RC   ECO:0000313|Proteomes:UP000030636};
RX   PubMed=25614573;
RA   Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Stevens M.J.,
RA   Jans C.;
RT   "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool Sample of
RT   an Anemic Kenyan Infant.";
RL   Genome Announc. 3:0-0(2015).
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; CP007457; AIZ16815.1; -; Genomic_DNA.
DR   RefSeq; WP_039172535.1; NZ_CP007457.1.
DR   AlphaFoldDB; A0A0A7IC61; -.
DR   STRING; 1447715.AH67_07820; -.
DR   GeneID; 61076409; -.
DR   KEGG; bpsp:AH67_07820; -.
DR   HOGENOM; CLU_013748_3_3_11; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000030636; 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:AIZ16815.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030636};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          20..132
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          209..338
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          414..549
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   590 AA;  63378 MW;  688B07A5EA155106 CRC64;
     MTDETTTTQP QEQNLTDSPH YLAQALMANG IKNMYGVVGI PVTDFARIAQ GMGMRFIGMR
     HEEDAVNAAA AEGFLTGKPA VALTVSAPGF LNGLAAMLEA TTNGFPVIMI GGSSTRHVVD
     MHEGEYEGLD QMNYAKAFCK ESFRIDKIED IPLAVARAMH IACSGRPGAV YIDFPDDAVA
     QTMDKDEAAA KLWTANQPNP AMPPAQASID EALKLLSEAK NPLMVVGKGA ALAQAEDELK
     EFVSKTDIPF QPMSMAKGLI PDDDPHCTAS ARGLALRTAD VVLLVGARLN WMLNFGEGKE
     WNPNVKFIQI EIDPNEIENA RPIACPVVGD IKSAMTMLNA GLEKTPFKAS AEWLSAIQAD
     SKQNDEKFAA RINSGKVPMG HYDALGAIKK VYDQHKDVII TNEGANTLDD CRNIIDIYQP
     RHRLDCGTWG VMGCAVGYSI GAAVSTGKQV LYIGGDSGFG FDGMEVEVAC RYNLPITFVV
     LNNGGIYRGD FENLGNDGDP SPLTLTYDAH YEKMIEAFGG KGYYATTPDE VEQMVGEAVA
     SGKPSFVHVQ LADYAGKESG HISNLNPKPV VGPLATSEVT ADPYIEGAHM
//