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Database: UniProt
Entry: A0A1B7JUF0_9GAMM
LinkDB: A0A1B7JUF0_9GAMM
Original site: A0A1B7JUF0_9GAMM 
ID   A0A1B7JUF0_9GAMM        Unreviewed;       567 AA.
AC   A0A1B7JUF0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:OAT51492.1};
DE            EC=4.1.1.8 {ECO:0000313|EMBL:OAT51492.1};
GN   ORFNames=M998_2107 {ECO:0000313|EMBL:OAT51492.1};
OS   Providencia heimbachae ATCC 35613.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1354272 {ECO:0000313|EMBL:OAT51492.1, ECO:0000313|Proteomes:UP000078224};
RN   [1] {ECO:0000313|EMBL:OAT51492.1, ECO:0000313|Proteomes:UP000078224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35613 {ECO:0000313|EMBL:OAT51492.1,
RC   ECO:0000313|Proteomes:UP000078224};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (APR-2016) 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:OAT51492.1}.
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DR   EMBL; LXEW01000031; OAT51492.1; -; Genomic_DNA.
DR   RefSeq; WP_068437963.1; NZ_LXEW01000031.1.
DR   AlphaFoldDB; A0A1B7JUF0; -.
DR   GeneID; 79029933; -.
DR   PATRIC; fig|1354272.4.peg.2139; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000078224; 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:OAT51492.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078224};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          11..126
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          408..543
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   567 AA;  60423 MW;  AA857625A71681CD CRC64;
     MSADQTQNLT DGMHIIVDAL KKNGIDTIYG VVGIPVTDMA RHAQAEGIRY IGFRHEQSAG
     NAAAISGFIT QKPGICLTVS APGFLNGLVA LANATTNGFP MIQISGSSDR AIIDLQQGDY
     EELDQMNTAK PFVKASYRVN KPEDLGIALA RAIRASVSGR PGGVYLDLTT EVLAAVMDKD
     EADKTIFVVE DPAPRQLPSP ASVNKALKLL ASAKRPLIIL GKGAAYAQAD DNIRQFIETT
     GIPYLPMSMA KGLLPDTHPQ SAASARSYAL SSADVVVLMG ARLNWLLDHG KGKHWSSETQ
     FIQLDIEPTE IDSNRPITAP IVGDIYSSIE ALLAGLKSTP VKSPNDWLAS IDEHKKANVE
     KMASKLNTDT SPMNYFNALR AIRDVLVDHK DAYVVNEGAN TLDNGRNIID MYEPRKRLDC
     GTWGVMGVGM GYAVGAAVTS GKPVVAIEGD SAFGFSGMEI DTICRYKLPV TILIFNNGGI
     YRGDGVNLHG DQDPSPTSLM GAARYDKMIE AFGGIGYNAT TPAEIQQALK AGLTSGNPTL
     INVVIDPAVG TESGHIGNLN PKSVVKN
//
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