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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//