ID   PCL_RHOCB               Reviewed;         384 AA.
AC   O69140; D5AR17;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=4-coumarate--CoA ligase;
DE            Short=4CL;
DE            EC=6.2.1.12;
DE   AltName: Full=4-coumaroyl-CoA synthase;
GN   Name=pcl; OrderedLocusNames=RCAP_rcc01063;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RA   Jiang Z., Bauer E.C.;
RT   "Genetic characterization of photoactive yellow protein from Rhodobacter
RT   capsulatus.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
CC   -!- FUNCTION: Converts p-coumaric acid into p-coumaryl CoA. This is
CC       necessary for the activation of the photoactive yellow protein (PYP)
CC       chromophore (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC17429.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF064095; AAC17429.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001312; ADE84823.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69140; -.
DR   SMR; O69140; -.
DR   STRING; 272942.RCAP_rcc01063; -.
DR   PRIDE; O69140; -.
DR   EnsemblBacteria; ADE84823; ADE84823; RCAP_rcc01063.
DR   KEGG; rcp:RCAP_rcc01063; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_660180_0_0_5; -.
DR   OMA; VPAHHIY; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR012743; 4_coum_CoA_lig.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02372; 4_coum_CoA_lig; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism;
KW   Reference proteome.
FT   CHAIN           1..384
FT                   /note="4-coumarate--CoA ligase"
FT                   /id="PRO_0000193044"
SQ   SEQUENCE   384 AA;  40942 MW;  D9184B69E58A1466 CRC64;
     MVRRLLISLI RAEARRGRNQ ILPEAAFTGD PRIDEEGLGF DSLARLDLIG AVRDFFDLSR
     TGIEDYVYVE PTLQGWIDRI MQHFDLLAAR SETAQAVFRT SGSTGTPKPI PHPWPKLMRE
     AASMARDQGL VPAPGGAVIG LVPAHHLFGC LFTALLPELA GAALRDLTAA PPASALRTAQ
     PGDLIIATPH LWAHLGAAGA FPPGLRGVSS GAPMPDALWH SLLAAGLEDL TEVYGASETG
     GIGLRRAPGA AFTLLPFLSR SADDGISDGP APLPLQDRLR WTGPVRFVIE GRLDQALQVG
     GVNVRLGHVK SVLEAEPGVE ALALRLGGDR LKAFVVCAAD AEAGLEARLR ARAEAGLDAP
     ARPQHYRFGR ALPLTREGKA RDWD