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MTND1_PHYPA
ID   MTND1_PHYPA             Reviewed;         194 AA.
AC   A9SDW6;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Acireductone dioxygenase 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE   AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=ARD' 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=Fe-ARD 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE            EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_03154};
DE   AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=ARD 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=Ni-ARD 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE            EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_03154};
GN   ORFNames=PHYPADRAFT_128349;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
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_03154}.
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_03154};
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_03154};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC       Note=Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes
CC       an acireductone dioxygenase reaction producing 2-keto-4-
CC       methylthiobutyrate, while nickel-binding promotes an acireductone
CC       dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
CC       {ECO:0000255|HAMAP-Rule:MF_03154};
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_03154}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}.
CC   -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC       {ECO:0000255|HAMAP-Rule:MF_03154}.
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DR   EMBL; DS544958; EDQ70527.1; -; Genomic_DNA.
DR   RefSeq; XP_001764545.1; XM_001764493.1.
DR   AlphaFoldDB; A9SDW6; -.
DR   SMR; A9SDW6; -.
DR   STRING; 3218.PP1S69_28V6.1; -.
DR   EnsemblPlants; Pp3c14_23430V3.1; Pp3c14_23430V3.1; Pp3c14_23430.
DR   Gramene; Pp3c14_23430V3.1; Pp3c14_23430V3.1; Pp3c14_23430.
DR   eggNOG; KOG2107; Eukaryota.
DR   HOGENOM; CLU_090154_0_1_1; -.
DR   InParanoid; A9SDW6; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000006727; Chromosome 14.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:RHEA.
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:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
DR   CDD; cd02232; cupin_ARD; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_03154; Salvage_MtnD_euk; 1.
DR   InterPro; IPR004313; ARD.
DR   InterPro; IPR027496; ARD_euk.
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; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW   Methionine biosynthesis; Nickel; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..194
FT                   /note="Acireductone dioxygenase 1"
FT                   /id="PRO_0000414342"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         87
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         89
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         89
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         93
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         93
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         132
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         132
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
SQ   SEQUENCE   194 AA;  23184 MW;  4D9143E849B67A34 CRC64;
     MEAWYMDDSA DDQRKPHHRS PPEYVSLEKL AELGVLHWVL DADSFETDPE LQRIRKERGY
     NYEDFIEVSP ERLANYETKI KNFYEEHMHT DEEIRYCLDG SGYFDIRDPE DRWIRIWVKK
     GDMIVLPAGS YHRFTLDENN YLKAMRLFVG EPVWTPYNRP QDEHPVRKDY INNFLKTHLD
     KIDVSLSTQH AATA
 
 
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