3MDO_PSEAE
ID 3MDO_PSEAE Reviewed; 201 AA.
AC Q9I0N5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=3-mercaptopropionate dioxygenase {ECO:0000303|PubMed:26272617};
DE Short=3MDO {ECO:0000303|PubMed:26272617};
DE Short=p3MDO {ECO:0000303|PubMed:26272617};
DE EC=1.13.11.91 {ECO:0000269|PubMed:26272617};
GN OrderedLocusNames=PA2602 {ECO:0000312|EMBL:AAG05990.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) IN COMPLEX WITH IRON, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26272617; DOI=10.1074/jbc.m114.635672;
RA Tchesnokov E.P., Fellner M., Siakkou E., Kleffmann T., Martin L.W.,
RA Aloi S., Lamont I.L., Wilbanks S.M., Jameson G.N.;
RT "The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-
RT mercaptopropionate dioxygenase.";
RL J. Biol. Chem. 290:24424-24437(2015).
CC -!- FUNCTION: Thiol dioxygenase that catalyzes the dioxygenation of 3-
CC mercaptopropionate (3-MPA) to 3-sulfinopropionate (3-SPA). To a lesser
CC extent (40-fold lower efficiency), is also able to oxidize cysteine to
CC cysteine sulfinate (CSA). Cannot use N-acetyl-L-cysteine, homocysteine,
CC and cysteamine as substrates. The physiological role of this enzyme is
CC unclear. {ECO:0000269|PubMed:26272617}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfanylpropanoate + O2 = 3-sulfinopropanoate + H(+);
CC Xref=Rhea:RHEA:53776, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:86386, ChEBI:CHEBI:137673; EC=1.13.11.91;
CC Evidence={ECO:0000269|PubMed:26272617};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:26272617};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:26272617};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for 3-mercaptopropionate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:26272617};
CC KM=8 mM for cysteine (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:26272617};
CC Note=kcat is 0.11 sec(-1) with 3-mercaptopropionate as substrate.
CC kcat is 0.021 sec(-1) with cysteine as substrate (at 37 degrees
CC Celsius). {ECO:0000269|PubMed:26272617};
CC -!- SUBUNIT: Forms homodimer in the crystal; however, there is no evidence
CC that the dimer exists under physiological conditions or has biological
CC significance. {ECO:0000269|PubMed:26272617}.
CC -!- INDUCTION: Is expressed in low levels (at protein level).
CC {ECO:0000269|PubMed:26272617}.
CC -!- MISCELLANEOUS: Does not contain a cysteine-tyrosine cross-link observed
CC in all mammalian cysteine dioxygenase (CDO) structures.
CC {ECO:0000269|PubMed:26272617}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG05990.1; -; Genomic_DNA.
DR PIR; E83319; E83319.
DR RefSeq; NP_251292.1; NC_002516.2.
DR RefSeq; WP_003113364.1; NZ_QZGE01000008.1.
DR PDB; 3USS; X-ray; 2.70 A; A/B=1-201.
DR PDB; 4TLF; X-ray; 2.14 A; A/B/C/D=1-201.
DR PDBsum; 3USS; -.
DR PDBsum; 4TLF; -.
DR AlphaFoldDB; Q9I0N5; -.
DR SMR; Q9I0N5; -.
DR STRING; 287.DR97_5425; -.
DR PaxDb; Q9I0N5; -.
DR DNASU; 882308; -.
DR EnsemblBacteria; AAG05990; AAG05990; PA2602.
DR GeneID; 882308; -.
DR KEGG; pae:PA2602; -.
DR PATRIC; fig|208964.12.peg.2723; -.
DR PseudoCAP; PA2602; -.
DR HOGENOM; CLU_118472_1_0_6; -.
DR InParanoid; Q9I0N5; -.
DR OMA; DHRVWGL; -.
DR PhylomeDB; Q9I0N5; -.
DR BioCyc; PAER208964:G1FZ6-2641-MON; -.
DR BRENDA; 1.13.11.20; 5087.
DR BRENDA; 1.13.11.91; 231.
DR SABIO-RK; Q9I0N5; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR010300; CDO_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR12918; PTHR12918; 1.
DR Pfam; PF05995; CDO_I; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..201
FT /note="3-mercaptopropionate dioxygenase"
FT /id="PRO_0000436011"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26272617,
FT ECO:0007744|PDB:3USS"
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26272617,
FT ECO:0007744|PDB:3USS"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26272617,
FT ECO:0007744|PDB:3USS"
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:4TLF"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:4TLF"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4TLF"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:4TLF"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4TLF"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4TLF"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4TLF"
SQ SEQUENCE 201 AA; 22548 MW; EDD64FEAA70FC425 CRC64;
MSSILRLDRL RQFIGELATL LDSRPDESTL LAQAHPLLAE LVHQDDWLPE DCARPDPQRY
QQYLLHVDSR QRFSVVSFVW GPGQITPVHD HRVWGLIGML RGAEYSQPYA FDAGGRPHPS
GARRRLEPGE VEALSPRIGD VHQVSNAFSD RTSISIHVYG ANIGAVRRAV FSAEGEEKPF
ISGYSNSRLP NIWDLSKENP A
