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Database: UniProt
Entry: B1M0K8_METRJ
LinkDB: B1M0K8_METRJ
Original site: B1M0K8_METRJ 
ID   B1M0K8_METRJ            Unreviewed;       581 AA.
AC   B1M0K8;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:ACB27530.1};
GN   OrderedLocusNames=Mrad2831_5585 {ECO:0000313|EMBL:ACB27530.1};
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB27530.1, ECO:0000313|Proteomes:UP000006589};
RN   [1] {ECO:0000313|EMBL:ACB27530.1, ECO:0000313|Proteomes:UP000006589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC   0-1 {ECO:0000313|Proteomes:UP000006589};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) 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; CP001001; ACB27530.1; -; Genomic_DNA.
DR   RefSeq; WP_012322472.1; NC_010505.1.
DR   AlphaFoldDB; B1M0K8; -.
DR   STRING; 426355.Mrad2831_5585; -.
DR   KEGG; mrd:Mrad2831_5585; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_3_5; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000006589; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008949; F:oxalyl-CoA decarboxylase activity; IEA:InterPro.
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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          23..139
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          214..345
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          413..554
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   581 AA;  61398 MW;  83CB12A1A93BDE6A CRC64;
     MTAVAKIVHT APEVEAEPDL TDGFHLVIDA LKLNGIDTIY GVPGIPITDL GRMAQAEGMR
     VISFRHEQHA GNAAAIAGFL TQKPGICLTV SAPGFLNGLT ALANATTNCF PMILISGSSE
     REIVDLQQGD YEEMDQLAIA KPLCKAAFRV LHAADIGIGV ARAIRAACSG RPGGVYLDLP
     AKLFSQVMDA EAGQKSLVKV IDPAPAQHPA PEAIARALEV LKSAKRPLIV LGKGAAYAQA
     DEAIRALVET SGIPYVPMSM AKGLLPDTHP LSAGAARSTA LKDSDVVLLI GARLNWLLSH
     GKGKSWGEPG STKFIQIDIE PREMDSNVEI VAPVVGDIAS CVQALLDGMG QGWQQPPSDW
     IETLKTKREA NIAKMAPKLM SNASPMNFHA ALGALRTIIK ERPDAILVNE GANTLDLARG
     IIDMYQPRKR LDVGTWGIMG IGMGFAVAAA VETGKPVLCV EGDSAFGFSG MEVETICRYG
     LPVCIVVFNN NGIYRGTDTD PTGRDPATTV FVPDSRYDRM IEAFGGVGYH VTTPDELTRA
     VNEAMNSGRP ALVNAVIDPA AGSESGNIGS LNPQSGIKKK K
//
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