ID   HCAD_PHOLL              Reviewed;         394 AA.
AC   Q7N4V5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=plu2209;
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       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; BX571866; CAE14502.1; -; Genomic_DNA.
DR   RefSeq; WP_011146461.1; NC_005126.1.
DR   AlphaFoldDB; Q7N4V5; -.
DR   SMR; Q7N4V5; -.
DR   STRING; 243265.plu2209; -.
DR   EnsemblBacteria; CAE14502; CAE14502; plu2209.
DR   GeneID; 24166430; -.
DR   KEGG; plu:plu2209; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_0_6; -.
DR   OMA; IATYPYH; -.
DR   OrthoDB; 1149616at2; -.
DR   BioCyc; PLUM243265:PLU_RS11030-MON; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000002514; 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;
KW   Reference proteome.
FT   CHAIN           1..394
FT                   /note="3-phenylpropionate/cinnamic acid dioxygenase
FT                   ferredoxin--NAD(+) reductase component"
FT                   /id="PRO_0000333727"
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   394 AA;  43579 MW;  F5977C83A10EBBC9 CRC64;
     MRNQTFIIVG AGQAGAMAAA TLRQQQFDGD IILIGKEYHA PYERPILSKD YLINPEEAPK
     YLFSEDFYLE KQIDLRIGQL VSQIMPSKHC VVLENGGKLR YDKLLLTMGA RARRFPLLDQ
     LGENIYTLRT LDDAQRLRQA VKKDKRILIV GGGVIGLELA ATSCELGANV TVIEQADNIM
     GRCAPPLLQD YLLNRHQEKG VQFFLDTNIV SAQKQGSELV LILNTGEKVI GDIIIYGIGA
     EFRDQLAADA GLVTDGGIVI DSRCQTSEPD IFAAGDVCLQ REPLTGDLQR RETWENANRQ
     ATIAAHAMMG LAPPQPGAPW FWTDQWGINI QMVGNMQAEE WHIQGDLQSD KAILFGTENE
     VLVGAVAINQ GREMRNLRKL LANPAQVVSG VEWA