HCAD_SHISS
ID HCAD_SHISS Reviewed; 400 AA.
AC Q3YZ11;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component {ECO:0000255|HAMAP-Rule:MF_01651};
DE EC=1.18.1.3 {ECO:0000255|HAMAP-Rule:MF_01651};
GN Name=hcaD {ECO:0000255|HAMAP-Rule:MF_01651}; OrderedLocusNames=SSON_2624;
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. {ECO:0000255|HAMAP-
CC Rule:MF_01651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01651};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01651};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01651}.
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_01651}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000255|HAMAP-Rule:MF_01651}.
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DR EMBL; CP000038; AAZ89251.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YZ11; -.
DR SMR; Q3YZ11; -.
DR EnsemblBacteria; AAZ89251; AAZ89251; SSON_2624.
DR KEGG; ssn:SSON_2624; -.
DR HOGENOM; CLU_003291_4_0_6; -.
DR OMA; IATYPYH; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000002529; Chromosome.
DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01651; HcaD; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR023744; HcaD.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..400
FT /note="3-phenylpropionate/cinnamic acid dioxygenase
FT ferredoxin--NAD(+) reductase component"
FT /id="PRO_0000333729"
FT BINDING 5..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01651"
FT BINDING 146..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01651"
SQ SEQUENCE 400 AA; 43976 MW; D7AD540F7B75272F CRC64;
MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS MLLEDSPQLQ
QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH WDQLFIAIGA AARPLPLLDA
LGERCFTLRH AGDAARLREV LQPERSVVIV GAGTIGLELA ASATQRRCKV TVIELAATVM
GRNAPPPVQR YLLQRHQQAG VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS
ANEQLAREAN LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ
IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA IWFNLQNGVL
IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL
