ID L0LZS8_ENTBF Unreviewed; 453 AA.
AC L0LZS8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01648};
DE EC=1.14.12.19 {ECO:0000256|HAMAP-Rule:MF_01648};
GN Name=hcaE {ECO:0000256|HAMAP-Rule:MF_01648};
GN OrderedLocusNames=D782_1131 {ECO:0000313|EMBL:AGB77153.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB77153.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB77153.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB77153.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
CC -!- FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase.
CC Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-
CC phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-
CC dihydrodiol (CI-dihydrodiol), respectively. {ECO:0000256|HAMAP-
CC Rule:MF_01648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + H(+) + NADH + O2 = (2E)-3-(cis-5,6-
CC dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD(+);
CC Xref=Rhea:RHEA:25058, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15669, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61451; EC=1.14.12.19; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpropanoate + H(+) + NADH + O2 = 3-(cis-5,6-
CC dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+);
CC Xref=Rhea:RHEA:20357, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:51057, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:60087; EC=1.14.12.19; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01648};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01648};
CC Note=Binds 1 Fe cation. {ECO:0000256|HAMAP-Rule:MF_01648};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01648};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01648};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000256|HAMAP-Rule:MF_01648}.
CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC subunits of the hydroxylase component (HcaE and HcaF), a ferredoxin
CC (HcaC) and a ferredoxin reductase (HcaD). {ECO:0000256|HAMAP-
CC Rule:MF_01648}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751,
CC ECO:0000256|HAMAP-Rule:MF_01648}.
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; CP003938; AGB77153.1; -; Genomic_DNA.
DR AlphaFoldDB; L0LZS8; -.
DR STRING; 693444.D782_1131; -.
DR KEGG; ebf:D782_1131; -.
DR PATRIC; fig|693444.3.peg.1078; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_6; -.
DR OrthoDB; 9769355at2; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000011002; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR HAMAP; MF_01648; HcaE; 1.
DR InterPro; IPR020875; HcaE.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_01648};
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01648};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW Rule:MF_01648};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01648};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01648};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01648};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01648};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01648}; Reference proteome {ECO:0000313|Proteomes:UP000011002}.
FT DOMAIN 44..142
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01648"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01648"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01648"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01648"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01648"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01648"
SQ SEQUENCE 453 AA; 51068 MW; 82FBBBD670D3043D CRC64;
MTTKTPVDIY SLIDTHNGSV TPRIYTDPDI YQLELERIFG RCWLFLAHES QIPKAGDFFN
TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNT KAFTCPYHGW SYGINGELID
VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFANWDTSA PPLLDYLGDM KWYLDGMLDR
REGGTEIVGG VQKWVINCNW KFPAEQFASD QYHALFSHAS AVQVLGAKED GSDKHLGDGQ
TARPVWETAK DALQFGQDGH GSGFFFTEKP DANVWVDGAV SSYYRETYDE AEQRLGKVRA
LRLAGHNNIF PTLSWLNGTA TLRVWHPRGP DQVEVWAFCI TDKAASDEVK AAFENSATRA
FGPAGFLEQD DSENWCEIQK LLKGNKARNS QLCLQMGLGQ EKRREDGIPG ITNYIFSETA
ARGMYQRWAD LLASETWQEV DEKTAAYQQE VMK
//
