MTND_BACAN
ID MTND_BACAN Reviewed; 170 AA.
AC Q81MI9; Q6HTY9; Q6KN69;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
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};
GN OrderedLocusNames=BA_4258, GBAA_4258, BAS3949;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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; AE016879; AAP27979.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33375.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56250.1; -; Genomic_DNA.
DR RefSeq; NP_846493.1; NC_003997.3.
DR RefSeq; WP_000057328.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030199.1; NC_005945.1.
DR PDB; 4QGL; X-ray; 2.61 A; A=1-170.
DR PDB; 4QGM; X-ray; 2.97 A; A=1-170.
DR PDBsum; 4QGL; -.
DR PDBsum; 4QGM; -.
DR AlphaFoldDB; Q81MI9; -.
DR SMR; Q81MI9; -.
DR IntAct; Q81MI9; 1.
DR STRING; 260799.BAS3949; -.
DR DNASU; 1088831; -.
DR EnsemblBacteria; AAP27979; AAP27979; BA_4258.
DR EnsemblBacteria; AAT33375; AAT33375; GBAA_4258.
DR GeneID; 45023929; -.
DR KEGG; ban:BA_4258; -.
DR KEGG; bar:GBAA_4258; -.
DR KEGG; bat:BAS3949; -.
DR PATRIC; fig|198094.11.peg.4228; -.
DR eggNOG; COG1791; Bacteria.
DR HOGENOM; CLU_125400_0_0_9; -.
DR OMA; TTHWFDM; -.
DR UniPathway; UPA00904; UER00878.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; IEA:UniProtKB-UniRule.
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 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Dioxygenase; Iron; Metal-binding;
KW Methionine biosynthesis; Nickel; Oxidoreductase; Reference proteome.
FT CHAIN 1..170
FT /note="Acireductone dioxygenase"
FT /id="PRO_0000162939"
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 101
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 101
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 105
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 105
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 144
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT BINDING 144
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT SITE 98
FT /note="May play a role in metal incorporation in vivo"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT SITE 104
FT /note="May play a role in transmitting local conformational
FT changes"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT SITE 107
FT /note="Important to generate the dianion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4QGL"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4QGM"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4QGL"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4QGL"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4QGL"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4QGL"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4QGL"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:4QGL"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4QGM"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:4QGL"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:4QGL"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:4QGL"
SQ SEQUENCE 170 AA; 19548 MW; 9BF1BA3A8079B976 CRC64;
MAQIRIHEVN TRIENEVKVS KFLQEEGVLY EKWNISKLPP HLNENYSLTD ENKAEILAVF
SKEIADVSAR RGYKAHDVIS LSNSTPNLDE LLINFQKEHH HTDDEVRFIV SGHGIFAIEG
KDGTFFDVEL EPGDLISVPE NARHYFTLQD DRQVVAIRIF VTTEGWVPIY
