ID A0A3N2MDG6_9BACT Unreviewed; 558 AA.
AC A0A3N2MDG6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:ROT08138.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:ROT08138.1};
GN ORFNames=EEL33_05890 {ECO:0000313|EMBL:ROT08138.1};
OS Muribaculaceae bacterium Isolate-037 (Harlan).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486461 {ECO:0000313|EMBL:ROT08138.1, ECO:0000313|Proteomes:UP000275399};
RN [1] {ECO:0000313|EMBL:ROT08138.1, ECO:0000313|Proteomes:UP000275399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-037 (Harlan) {ECO:0000313|Proteomes:UP000275399};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
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:ROT08138.1}.
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DR EMBL; RIAZ01000005; ROT08138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2MDG6; -.
DR Proteomes; UP000275399; 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 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; 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 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:ROT08138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275399};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 59708 MW; F502EC83B6C062C8 CRC64;
MYVLARALKN IGIDNVYGLV GIPITEAAYL IQGQGIRFVG FRHEQQAGMA AATEGYLTGK
PGVLMTVSSL GFMNGLTATA NATVNCYPMI QISGASDPAM VDMNMGTYEQ LDQFNTAKPL
VKAAFRCTYA KDIPAAVYRA YRAAVSGRPG GVYIDMTTPA LGEIMNKVDA DKLFYTPVDI
YSPVAPNSRS VERAVEILTS AKRPAILLGK GAAYARLEDK IKTLVEKYQI PYLPMSMAKG
IMPDDGPLSA LSCRSTIMEK SDVVMVIGAR LNWMLSFGKG KWNPDMKFIQ LDVAPEEIDV
NVPIAAPVVG DMGLSMDAIL DALDGKSMAT DSDWVSGLQA EAKIKNAKFA KRFEEAKSMM
PMHHMTALSA IKPILEANPD VILINEGANT LDDTRDAVNM SLPRHRVDCA TWAIMGMGMG
SAIGAAVATG KSVVAIEGDS AFGFSGMDFS TICRFNLPVT VVIFNNGGIY NGIGVPMDKT
TDPAPTTLDV RARYDKLGDA FGAQTFYVTT PEQLSEALKT GIASKKPTLI DVQLAADSGK
ESGHIGYLNP APLQSITV
//
