MTND_XANCP
ID MTND_XANCP Reviewed; 188 AA.
AC Q8P9N4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE AltName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE Short=DHK-MTPene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
DE Short=ARD' {ECO:0000255|HAMAP-Rule:MF_01682};
DE Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_01682};
DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
DE Short=ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_01682};
GN Name=mtnD {ECO:0000255|HAMAP-Rule:MF_01682}; OrderedLocusNames=XCC1819;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Catalyzes 2 different reactions between oxygen and the
CC acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)
CC depending upon the metal bound in the active site. Fe-containing
CC acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-
CC methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine
CC in the methionine recycle pathway. Ni-containing acireductone
CC dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and
CC formate, and does not lie on the methionine recycle pathway.
CC {ECO:0000255|HAMAP-Rule:MF_01682}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-
CC (methylsulfanyl)propanoate + CO + formate + 2 H(+);
CC Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016,
CC ChEBI:CHEBI:49252; EC=1.13.11.53; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01682};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-
CC methylsulfanyl-2-oxobutanoate + formate + 2 H(+);
CC Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252;
CC EC=1.13.11.54; Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC Note=Binds 1 Fe(2+) cation per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_01682};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC Note=Binds 1 nickel ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01682};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 5/6. {ECO:0000255|HAMAP-Rule:MF_01682}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01682}.
CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC {ECO:0000255|HAMAP-Rule:MF_01682}.
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DR EMBL; AE008922; AAM41108.1; -; Genomic_DNA.
DR RefSeq; NP_637184.1; NC_003902.1.
DR RefSeq; WP_011036989.1; NC_003902.1.
DR AlphaFoldDB; Q8P9N4; -.
DR SMR; Q8P9N4; -.
DR STRING; 340.xcc-b100_2106; -.
DR EnsemblBacteria; AAM41108; AAM41108; XCC1819.
DR GeneID; 58013632; -.
DR KEGG; xcc:XCC1819; -.
DR PATRIC; fig|190485.4.peg.1940; -.
DR eggNOG; COG1791; Bacteria.
DR HOGENOM; CLU_125400_0_0_6; -.
DR OMA; TTHWFDM; -.
DR UniPathway; UPA00904; UER00878.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR GO; GO:0006555; P:methionine metabolic process; IBA:GO_Central.
DR CDD; cd02232; cupin_ARD; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_01682; Salvage_MtnD; 1.
DR InterPro; IPR004313; ARD.
DR InterPro; IPR023956; ARD_bac.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR23418; PTHR23418; 1.
DR Pfam; PF03079; ARD; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Dioxygenase; Iron; Metal-binding;
KW Methionine biosynthesis; Nickel; Oxidoreductase; Reference proteome.
FT CHAIN 1..188
FT /note="Acireductone dioxygenase"
FT /id="PRO_0000359247"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 97
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 99
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 99
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 103
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 103
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 141
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 141
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT SITE 96
FT /note="May play a role in metal incorporation in vivo"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT SITE 102
FT /note="May play a role in transmitting local conformational
FT changes"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT SITE 105
FT /note="Important to generate the dianion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
SQ SEQUENCE 188 AA; 21402 MW; 47A061B6CF54CBD4 CRC64;
MSRLRIFADS NPTTPHFDSR DGEQIATELR KIGVTFERWH ASQPVEPGAS PEQVMAAYRA
DIDRISAERG FKTVDVVSIA PDNPKREEMR AKFLDEHFHK EDEVRFFVAG SGLFTLHVDA
QVYEIECVKD DLIAVPDSTL HWFDMGPEPH FVAIRFFTEP DGWVGHFTGT EIAKQFPRYA
PEKPPKAS
