ID D4I3N6_ERWAC Unreviewed; 646 AA.
AC D4I3N6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Malonic semialdehyde oxidative decarboxylase {ECO:0000313|EMBL:CBA23832.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CBA23832.1};
GN Name=iolD {ECO:0000313|EMBL:CBA23832.1};
GN OrderedLocusNames=EAMY_3508 {ECO:0000313|EMBL:CBA23832.1};
OS Erwinia amylovora (strain CFBP1430).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA23832.1, ECO:0000313|Proteomes:UP000001841};
RN [1] {ECO:0000313|EMBL:CBA23832.1, ECO:0000313|Proteomes:UP000001841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841};
RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA Duffy B.;
RT "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT CFBP 1430 and comparison to other Erwinia spp.";
RL Mol. Plant Microbe Interact. 23:384-393(2010).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FN434113; CBA23832.1; -; Genomic_DNA.
DR RefSeq; WP_004160870.1; NC_013961.1.
DR AlphaFoldDB; D4I3N6; -.
DR STRING; 665029.EAMY_3508; -.
DR GeneID; 8913184; -.
DR KEGG; eam:EAMY_3508; -.
DR PATRIC; fig|665029.3.peg.3365; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_6; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000001841; Chromosome.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR CDD; cd02003; TPP_IolD; 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; IPR030817; Myo_inos_IolD.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:CBA23832.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 23..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..352
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 442..601
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 646 AA; 70454 MW; 19231C6FCFF78257 CRC64;
MGKIRLTTAQ ALVRFLDNQY LSVDGVESKF VKGIFAIFGH GNVLGLGQAL EQDSGDLRVY
QGRNEQGMAH AATGFAKQRL RREIIACTSS VGPGAANMLT AAATASANRI PLLLLPGDVF
ATRQPDPVLQ QVEQSHDLSI STNDAFRAVS KYWDRVSRPE QLMTACISAM RVLTDPAETG
AVTLSLPQDV QGEAYNYPDY FFQKRVHRLE RRLPTEGQLS DALALIAAKK RPMIICGGGV
KYSGAGDALR AFAERYQIPF AETQAGKGTI LSDHPLNVGG VGETGCLAAN LLAKEADLVI
GIGTRYSDFT TASKWIFHNP DVSYLNINVS NFDACKLDGV QVLADAREAL TAIGNRLAAT
GFQHGWGEKV PQARARMLKE AQRVYSVVYS GDDFVPEIDD DIDRAALYAE FNRLTGSFLT
QSSVLGTLNE HLPRDAVIVA AAGSLPGDLQ RMWRTTDDNG YHVEYGYSCM GYEVNAALGV
KLAEPQRDVY ALVGDGSFMM LHSELVTSIQ EGAKIHVILL DNMANGCINN LQMEHGMGSF
TTEFRFRDAE SGRLNGGLVP VDFAAIAAGY GCKTWRVTTL EQLHLALTAA QKETVSTLID
IKVLPKTMIH KYFSWWRVGG AQVSNSSRID AVAQMLNKHI DQAREY
//
