ID C4WS41_ACYPI Unreviewed; 181 AA.
AC C4WS41;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Acireductone dioxygenase {ECO:0000256|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=ARD' {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=Fe-ARD {ECO:0000256|HAMAP-Rule:MF_03154};
DE EC=1.13.11.54 {ECO:0000256|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=ARD {ECO:0000256|HAMAP-Rule:MF_03154};
DE Short=Ni-ARD {ECO:0000256|HAMAP-Rule:MF_03154};
DE EC=1.13.11.53 {ECO:0000256|HAMAP-Rule:MF_03154};
GN Name=ACYPI002479 {ECO:0000313|EMBL:BAH70711.1};
GN Synonyms=100161243 {ECO:0000313|EnsemblMetazoa:NP_001156109.1};
OS Acyrthosiphon pisum (Pea aphid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX NCBI_TaxID=7029 {ECO:0000313|EMBL:BAH70711.1};
RN [1] {ECO:0000313|EMBL:BAH70711.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LSR1 {ECO:0000313|EMBL:BAH70711.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:BAH70711.1};
RA Shigenobu S., Nakabachi A., Richards S.;
RT "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819};
RA Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S.,
RA Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V.,
RA Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V.,
RA Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L.,
RA Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A.,
RA Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L.,
RA Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J.,
RA Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D.,
RA Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A.,
RA Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H.,
RA Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R.,
RA James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B.,
RA Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A.,
RA Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H.,
RA Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J.,
RA Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E.,
RA Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B.,
RA Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q.,
RA Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A.,
RA Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L.,
RA Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M.,
RA Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W.,
RA Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H.,
RA Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S.,
RA Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C.,
RA Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C.,
RA Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M.,
RA Weinstock G., Gibbs R.A.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:NP_001156109.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
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:0000256|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:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00000428,
CC ECO:0000256|HAMAP-Rule:MF_03154};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03154};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03154}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03154}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03154}.
CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC {ECO:0000256|HAMAP-Rule:MF_03154}.
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DR EMBL; AK340037; BAH70711.1; -; mRNA.
DR RefSeq; NP_001156109.1; NM_001162637.2.
DR RefSeq; XP_016661935.1; XM_016806446.1.
DR AlphaFoldDB; C4WS41; -.
DR STRING; 7029.C4WS41; -.
DR EnsemblMetazoa; NM_001162637.2; NP_001156109.1; LOC100161243.
DR EnsemblMetazoa; XM_016806446.2; XP_016661935.1; LOC100161243.
DR GeneID; 100161243; -.
DR KEGG; api:100161243; -.
DR eggNOG; KOG2107; Eukaryota.
DR HOGENOM; CLU_090154_0_1_1; -.
DR InParanoid; C4WS41; -.
DR OMA; CEYGDLI; -.
DR OrthoDB; 130851at2759; -.
DR UniPathway; UPA00904; UER00878.
DR Proteomes; UP000007819; Unassembled WGS sequence.
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: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-UniRule.
DR CDD; cd02232; cupin_ARD; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 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; ACIREDUCTONE DIOXYGENASE; 1.
DR PANTHER; PTHR23418:SF0; ACIREDUCTONE DIOXYGENASE; 1.
DR Pfam; PF03079; ARD; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03154};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03154};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03154};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_03154};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03154};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03154}; Reference proteome {ECO:0000313|Proteomes:UP000007819}.
FT BINDING 90
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 90
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 92
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 92
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 96
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 96
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 136
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03154"
SQ SEQUENCE 181 AA; 21547 MW; 69A6B2B459ED1ABC CRC64;
MVQAWFMAEN WSGDQREEHH MQPPEFIELD TLYKLTLVEH FKVNESDPTN DKLLNSIKKE
RGYSYEDEIT CSKECLPNYE SKLKMFFEEH LHTDEEIRLV LEGSGYFDVR DGVNDRWIRI
KVEPGDLLII PKGIYHRFTL DTNNFIKAKR FFVGEPVWTP HNRPADDMNC RKEYLNQIIS
C
//
