ID D1P666_9GAMM Unreviewed; 567 AA.
AC D1P666;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:EFB71189.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:EFB71189.1};
GN Name=oxc {ECO:0000313|EMBL:EFB71189.1};
GN ORFNames=PROVRUST_07730 {ECO:0000313|EMBL:EFB71189.1};
OS Providencia rustigianii DSM 4541.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB71189.1, ECO:0000313|Proteomes:UP000005512};
RN [1] {ECO:0000313|EMBL:EFB71189.1, ECO:0000313|Proteomes:UP000005512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB71189.1,
RC ECO:0000313|Proteomes:UP000005512};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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:EFB71189.1}.
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DR EMBL; ABXV02000042; EFB71189.1; -; Genomic_DNA.
DR RefSeq; WP_006815729.1; NZ_GG703820.1.
DR AlphaFoldDB; D1P666; -.
DR STRING; 500637.PROVRUST_07730; -.
DR GeneID; 76390831; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_6; -.
DR Proteomes; UP000005512; 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 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:EFB71189.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 11..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 567 AA; 61126 MW; 953973397E7C8D80 CRC64;
MSTNQNQNLT DGMHIIIDAL KKNDIDTIYG VVGIPVTDMA RHAQAVGIRY IGFRHEQSAG
NAAAISGYIT QKPGICLTVS APGFLNGMVA LANATTNGFP MIQISGSSNR AIIDLQQGDY
EELDQMNIAK PFVKASYRVN KPEDLGIALA RAIRTSVSGR PGGVYLDLTT EVLAAVMDKD
EADKTIFKVE DPAPKQLPSP YSIKKALQLL ASAKQPLIIL GKGAAYAQAD EKIRQFVEET
GIPYLPMSMA KGLLPDNHPQ SAASARSYAL SNADVVVLMG ARLNWLLDHG KGKHWSPDTQ
FIQLDIEPTE IDSNRPISAP IVGDIDSSVE ALLTGLKSIP VKSPNEWLAT IDEHKKVNVE
KMATKLNTDT SPMNYFNALR AIRDVLVDHK DVYVVNEGAN TLDNARNIID MYQPRKRLDC
GTWGVMGVGM GYAVGASVTS GIPVVAIEGD SAFGFSGMEI ETICRYKLPV TILIFNNGGI
YRGDDKNLHG DTDPSPTVLM ADARYDKMIE AFGGIGYYAT TPQEIQQALK KGITSRSPTL
INVIIDPAVG TESGHIGNLN PKSVAGN
//
