HCAC_SHISS
ID HCAC_SHISS Reviewed; 106 AA.
AC Q3YZ13;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit {ECO:0000255|HAMAP-Rule:MF_01650};
GN Name=hcaC {ECO:0000255|HAMAP-Rule:MF_01650}; OrderedLocusNames=SSON_2622;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase,
CC that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into
CC 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-
CC dihydrodiol (CI-dihydrodiol), respectively. This protein seems to be a
CC 2Fe-2S ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01650}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01650};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01650};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01650}.
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_01650}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000255|HAMAP-Rule:MF_01650}.
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DR EMBL; CP000038; AAZ89249.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YZ13; -.
DR SMR; Q3YZ13; -.
DR EnsemblBacteria; AAZ89249; AAZ89249; SSON_2622.
DR KEGG; ssn:SSON_2622; -.
DR HOGENOM; CLU_055690_5_2_6; -.
DR OMA; TLECWLH; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000002529; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.102.10.10; -; 1.
DR HAMAP; MF_01650; HcaC; 1.
DR InterPro; IPR023739; HcaC.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Transport.
FT CHAIN 1..106
FT /note="3-phenylpropionate/cinnamic acid dioxygenase
FT ferredoxin subunit"
FT /id="PRO_0000333723"
FT DOMAIN 4..99
FT /note="Rieske"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01650"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01650"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01650"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01650"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01650"
SQ SEQUENCE 106 AA; 11329 MW; B83149F4126BB72D CRC64;
MNRIYACPVA DVPEGEALRI DTSPVIALFN VGGEFYAIND RCSHGNASMS EGYLEDDATV
ECPLHAASFC LKTGKALCLP ATDPLTTYPV HVEGGDIFID LPEAQP