ID B1ZBX8_METPB Unreviewed; 584 AA.
AC B1ZBX8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:ACB79321.1};
GN OrderedLocusNames=Mpop_1149 {ECO:0000313|EMBL:ACB79321.1};
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620 {ECO:0000313|EMBL:ACB79321.1, ECO:0000313|Proteomes:UP000007136};
RN [1] {ECO:0000313|EMBL:ACB79321.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJ001 {ECO:0000313|EMBL:ACB79321.1};
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., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-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; CP001029; ACB79321.1; -; Genomic_DNA.
DR RefSeq; WP_012453071.1; NC_010725.1.
DR AlphaFoldDB; B1ZBX8; -.
DR STRING; 441620.Mpop_1149; -.
DR KEGG; mpo:Mpop_1149; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000007136; 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 26..142
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 217..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 416..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 565..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 61784 MW; D0E3C0822DD9B7F6 CRC64;
MTVQAQNIDA ITAGAVPHEE AELTDGFHLV IDALKLNGIE TIYNVPGIPI TDLGRLAQAE
GLRVVSFRHE QNAGNAAAIA GFLTKKPGIC LTVSAPGFLN GLTALANATT NCFPMILISG
SSEREIVDLQ QGDYEEMDQL AIAKPLCKAA FRVLHAADIG IGVARAIRAA VSGRPGGVYL
DLPAKLFSQV IDADLGARSL VKVIDPAPAQ IPAPASVARA LDLLKGAERP LIILGKGAAY
AQADEAVRAL VEESGIPYVP MSMAKGLLPD THPLSAGAAR STALKDSDVV VLVGARLNWL
LSHGKGKTWG EPGSKRFIQI DIEPREMDSN VEIAAPLVGD IGSCVEALLE GIRKDWKGAP
ENWLQTIRTK REANIAKMAP KLMKNTSPMC FHSALGALRT VIKERPDAIL VNEGANTLDL
ARGIIDMYQP RKRLDVGTWG VMGIGMGFAV AAAVETGKPV LAVEGDSAFG FSGMEVETIC
RYDLPVCIVI FNNNGIYRGT DTDPTGRDPG TTVFVKDSRY DRMMEAFGGV GVNVTTPDEL
KRAVDAAMDS GKPTLINAVI DPAAGSESGN IGSLNPQSTL KKKK
//
