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 09-APR-2025, entry version 95.
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; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Rhodobacter group; 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 KEGG; rcp:RCAP_rcc01063; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_660180_0_0_5; -.
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; N-terminal domain of ligase-like; 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_dom.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR050237; ATP-dep_AMP-bd_enzyme.
DR NCBIfam; TIGR02372; 4_coum_CoA_lig; 1.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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
//
