HCAE_PHOLL
ID HCAE_PHOLL Reviewed; 453 AA.
AC Q7N4W0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01648};
DE EC=1.14.12.19 {ECO:0000255|HAMAP-Rule:MF_01648};
GN Name=hcaE {ECO:0000255|HAMAP-Rule:MF_01648}; OrderedLocusNames=plu2204;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01648};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01648};
CC Note=Binds 1 Fe cation. {ECO:0000255|HAMAP-Rule:MF_01648};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01648};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01648};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01648}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01648}.
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DR EMBL; BX571866; CAE14497.1; -; Genomic_DNA.
DR RefSeq; WP_011146456.1; NC_005126.1.
DR AlphaFoldDB; Q7N4W0; -.
DR SMR; Q7N4W0; -.
DR STRING; 243265.plu2204; -.
DR EnsemblBacteria; CAE14497; CAE14497; plu2204.
DR GeneID; 24166435; -.
DR KEGG; plu:plu2204; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_6; -.
DR OMA; AQVGYNE; -.
DR OrthoDB; 275867at2; -.
DR BioCyc; PLUM243265:PLU_RS11005-MON; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000002514; 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; -; 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; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..453
FT /note="3-phenylpropionate/cinnamic acid dioxygenase subunit
FT alpha"
FT /id="PRO_0000333705"
FT DOMAIN 43..141
FT /note="Rieske"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01648"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01648"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01648"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01648"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01648"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01648"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01648"
SQ SEQUENCE 453 AA; 51322 MW; 150ECAD0216477AE CRC64;
MTLSKDSDIY RLIDARAGRV TPQIYIDPEL YQLELERIFG RCWLFLAHQS QIPNPGDFFN
TYMGEDSVVV VRQKNGSVKA FLNQCRHRSM RVCYADSGNT RAFTCPYHGW SYGVDGRLID
VPLEACAYPH GLCKEQWGLQ EVPCVENYKG LIFGNWDTTA PSLIDYLGDM AWYLDGVLDR
REGGTEVIGG VQKWLINCNW KLPAEQFAGD QYHALFSHAS AVQVLSVKDG DDKKALGADQ
TSRPVWETAK DAVQFAQNGH GCGFFLTEKP DANVWVDGAV ARYYRETYAE AEQRLGKVRA
LRLAGHNNIF PTLSWLNGTA TMRVWHPRGP DQVEVWAFCI ADKAASPEVK AAFENSATRA
FGPAGFLEQD DSENWVEIQK VLRGYKARNS TLCMEMRLGQ ERVRDDGIPG VTNYVFSETV
ARGMYQRWAD LLTSETWDEI EEKSRVYQQE LVK
