ID A0A127JTH4_9BURK Unreviewed; 584 AA.
AC A0A127JTH4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Oxalyl-CoA decarboxylase {ECO:0000313|EMBL:AMO23215.1};
DE EC=4.1.1.8 {ECO:0000313|EMBL:AMO23215.1};
GN ORFNames=UC35_10325 {ECO:0000313|EMBL:AMO23215.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO23215.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO23215.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO23215.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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; CP010951; AMO23215.1; -; Genomic_DNA.
DR RefSeq; WP_061498921.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127JTH4; -.
DR PATRIC; fig|94132.3.peg.2103; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000070433; Chromosome.
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:AMO23215.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 25..139
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 216..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 416..558
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 584 AA; 61582 MW; 03405119D8F8DF91 CRC64;
MSSVLDTPAA TLQKIAAEPA ELTDGFHLVI DALKLNGIDT IYGLPGIPIT DLTRMAQAEG
MRVIAFRHEQ NAGNAAAAAG FLTQKPGICL TVSAPGFLNG LTALANATVN CFPMILISGS
SEREIVDLAQ GDYEEMDQLN VAKPFCKAAF RITYAHDIGI GIARAIRAAV SGRPGGVYLD
LPAKLFSQTM EALAGRNSLV KVVDPAPRQL PAPDTVKRAL DVIKGAKRPL ILLGKGAAYA
QADAEIRAFV EKSGIPYLPM SMAKGLLPDT HPQSAAAARS YVLQEADVVV LVGARLNWLL
SHGKGKTWGA DKGPKKFVQI DIAATEMDSN VPIDAPLVGD IGSCVSALVA GIGAGWAKPP
ADWLATIAER KDKNLSKMAA QLAQSPSPMN FHSALGAIRE IVKQNPDAMV VNEGANTLDF
ARSIVDMYQP RKRLDCGTWG IMGIGMGFAV AAAVETGKPV IAIEGDSAFG FSGMEVETIC
RYNLPVCIVV FNNNGVYKGT DKNPSGTADP APTVFVKDSR YDLMMEAFGG KGVTARTPQE
LTRAMEEAIA SGRPTLINAV IDETAGTESG RITNLNPAKA ATKK
//
