ID F6EF48_HOYSD Unreviewed; 328 AA.
AC F6EF48;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01653};
DE EC=1.13.11.16 {ECO:0000256|HAMAP-Rule:MF_01653};
DE AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01653};
GN Name=mhpB {ECO:0000256|HAMAP-Rule:MF_01653,
GN ECO:0000313|EMBL:AEF38627.1};
GN OrderedLocusNames=AS9A_0167 {ECO:0000313|EMBL:AEF38627.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF38627.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF38627.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage
CC of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid
CC into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-
CC ketononatrienedioate, respectively. {ECO:0000256|HAMAP-Rule:MF_01653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-
CC hydroxy-6-oxonona-2,4,7-trienedioate + H(+); Xref=Rhea:RHEA:25054,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:58642,
CC ChEBI:CHEBI:66888; EC=1.13.11.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001748, ECO:0000256|HAMAP-
CC Rule:MF_01653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-
CC oxonona-2,4-dienedioate + H(+); Xref=Rhea:RHEA:23840,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:46951,
CC ChEBI:CHEBI:66887; EC=1.13.11.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001843, ECO:0000256|HAMAP-
CC Rule:MF_01653};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01653};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005207, ECO:0000256|HAMAP-Rule:MF_01653}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_01653}.
CC -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00007030, ECO:0000256|HAMAP-Rule:MF_01653}.
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DR EMBL; CP002786; AEF38627.1; -; Genomic_DNA.
DR RefSeq; WP_013804979.1; NC_015564.1.
DR AlphaFoldDB; F6EF48; -.
DR STRING; 443218.AS9A_0167; -.
DR KEGG; asd:AS9A_0167; -.
DR eggNOG; COG3384; Bacteria.
DR HOGENOM; CLU_078149_0_0_11; -.
DR OrthoDB; 8673673at2; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000009235; Chromosome.
DR GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.830.10; LigB-like; 1.
DR HAMAP; MF_01653; MhpB; 1.
DR InterPro; IPR023789; DHPP/DHXA_dioxygenase.
DR InterPro; IPR004183; Xdiol_dOase_suB.
DR Pfam; PF02900; LigB; 1.
DR SUPFAM; SSF53213; LigB-like; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01653};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW Rule:MF_01653}; Iron {ECO:0000256|HAMAP-Rule:MF_01653};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01653};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT DOMAIN 6..305
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01653"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01653"
SQ SEQUENCE 328 AA; 35608 MW; 14401E19F2F9DDC2 CRC64;
MPVALVATSH SPLIGLNDPT TEIRDEVRGV LDDARAFVRD FDPELVVMFA PDHYNGFFYD
MMPPFCIGAS AHSVGDYGLP TGDLSVDKAA AYDIGASVLA QGVDLAISED MQVDHGFVQP
LLFLFDTLQS VPIVPIFINC VASPLGPARR SMDLGSAVGA ALADDDRRIL LVGSGGLSHD
PPVPRMEDAA PEVIERLLLR GRNPSTEQRA TREEKTVKAA RAYAAGEAGY RELNPEWDKL
VLDALSSGDF ARIVDHDNDW FVREGGHSSH EIRTWIAAYA ALSGQGPYQV QSRYYRPIKE
WFAGFSTTIA TPASALAHAR VSNKGVVR
//
