ID Q01KB0_ORYSA Unreviewed; 2391 AA.
AC Q01KB0;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=4-coumarate--CoA ligase {ECO:0000256|ARBA:ARBA00012959};
DE EC=6.2.1.12 {ECO:0000256|ARBA:ARBA00012959};
GN Name=OSIGBa0135C13.1 {ECO:0000313|EMBL:CAH66806.1};
OS Oryza sativa (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4530 {ECO:0000313|EMBL:CAH66806.1};
RN [1] {ECO:0000313|EMBL:CAH66806.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2] {ECO:0000313|EMBL:CAH66806.1}
RP NUCLEOTIDE SEQUENCE.
RA Han B.;
RT "Chromosome-wide comparison between domesticated rice subspecies indica and
RT japonica.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00034252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC Evidence={ECO:0000256|ARBA:ARBA00034252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + H(+) = (E)-4-coumaroyl-AMP +
CC diphosphate; Xref=Rhea:RHEA:72419, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:192348; Evidence={ECO:0000256|ARBA:ARBA00034219};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72420;
CC Evidence={ECO:0000256|ARBA:ARBA00034219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H(+);
CC Xref=Rhea:RHEA:72423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:192348, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72424;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CR855145; CAH66806.1; -; Genomic_DNA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08151; AOS; 1.
DR CDD; cd05931; FAAL; 1.
DR Gene3D; 1.10.405.20; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.1990; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR Pfam; PF00550; PP-binding; 2.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 3.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS51402; CATALASE_3; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1303..1327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1347..1371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1408..1427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1543..1563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1575..1599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1606..1627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2189..2210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2217..2243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1103..1177
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1196..1270
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1981..2001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2391 AA; 261715 MW; 470189277800E0AD CRC64;
MDPKRSIDDQ FSKLHPSLPV DTRIGIVGAG PSGLSAAYAL AKLGYRNVTL FEKCHTVSGM
CESIDIEEEL GSDFEEMDTH KLSLIDSQTG NIRDLEVAED YVSMVSLTLK LQDEANKSGR
AGLHALSGLA SDPTHEFLKQ NGINSMPKSV AYGYTASGYG FVQDMPYAFI QEFTRTSMAG
KIRRFKHGYM SMWERLSKSL PFEVFCDTQV LNVKRNSCGA NVTIKNNNGE KQVLEFDKII
LSGAVAFKNS KTYRSSSLTD GESEVVELNN LERELFSKVQ TIDYYTTVVK INGFEHIPKG
FYYFEEFMED PTTIGHPVAM QRFFADTNIF LFWSYGNSAD IKGSFVAKCV TDVVSSMGGN
VQKVILQRRF KYFPHVSSKD MKDGFYERLE SQLQGFQNTY YVGGLLAFEL TERNASYSIM
AVCKHFAIDG EGELTPYVKR LFPLSHNRNP SPPRDLGELE GVEFPDLPSL DGYLQYWGTH
KVTEKNVIYT WINEEGKLMN RRTYQELHGN ASYIAQKLLT STKPVIKPGD RVLLIHLPGL
EFIDAFFGCI RAGVIPVPVL PPDPMQSGGQ ALLKVENISK MCNAVAILST SSYHAAVRAG
YIKNIVTLAK RVQKCSAQWP DIPWIQTDSW IKNYRRSSDS FNSDTVLFTK PQPSDLCFLQ
FTSGSTGDAK GVMITHEGLI HNVKTMKKRY RSTSKTVLVS WLPQYHDMGL IGGLFTALVS
GGTSVLFSPM TFIRNPLLWL QTINDYHGTH SAGPNFAFEL VIRRLEAEKN KVYDLSSMVF
LMIAAEPVRQ KTVRRFIELT QPFGLSEGVL APGYGLAENC VYVTCAFGEC KPVFIDWQGR
VCCGYVEQDD TDTLIRIVDP DSLTEHQEDG VEGEIWISSP SSGVGYWGNS EMSQRTFFNQ
LKNHPNKKFT RTGDLGRTID GNLFITGRIK DLIIVAGRNI YSADVEKTVE SSSEVLRPGC
CAVVGIPEEV LAQKGISIPD SSDQVGLVVI AEVREGKAVS EEVVNNIKAR VVEEHGVAVA
SVKLIKPRTI CKTTSGKIRR FECMRQFVDN TLSLAKGNHV SKKKGLFRSL TTGTGMESKR
SLLRQTVDLT ISHWPKSQVK NSNEITEFLT QIVSEHTGIS KDKISLTDSL PSYGFDSIAV
VRAAQKLSDF LGVPVGAIDI FTASCISELA SFLENLVHKS QPQLAPWPKS KVKNSKEIIE
FLTKIVSDQT GIPKDKISPT NSLPSYGFDS IAVVQAAQKL SDFLGVPVGA IDIFTAGCIS
ELATFLENLA HKSQSQLAPG ASCYIEDETQ VDPMDAISPE FSVLGTGILQ LLALTYVCFV
LLLPAYLASS TYMSIFSTVS LVRSPLLSYL SSLVMAPIVW IFYISLTSLS LSILGKSFLQ
PNYVLIPDVS IWSVDFVKWW ALNKAQALAA KMLAVHLKGT IFLNYWFKMQ GARIGSSVVI
DTVDITDPSL LTVADGAVLA EGALVQGHEV CNEVLSFRPI WIGCEASIGP YAVLQKGTVV
EDGAVVPPLQ KTGAGKSTRR TSRTSVSIKK EAAKANMILE HLVSIYAVGI LGALSGAIVY
TLYTHLSGKA ASPLHFSFAC IAGAFHWLPA AITAYAVIVQ ETPTSALSFA LFTAFADLSY
GVILSILTSI TSRALAAKPG TKQNGIASLI HRRITISAHV RFAKMLSGTE AFCVYLRLLG
AKIGRHCSIR AINPVANPEL ISVGDGVHLG DFCNIVPGFY SKGGFTSAEI KVQENTVVGS
GSLLLPGCVL QENVILGALS VAPENAVLRR GGVYVGSQSP AMVKNTLLDE DERIEEMDQA
YKKIVGNLAA NLAITTMNVK SRYFHRIGVS GRGVLRMYEE IPSFPRHKIF ASGKSFPVIV
RHSNSLSADD DARLDARGAA VRILSDNDGE APLLDLTLKS GKAFYARTIA DFATWLVCGL
PAREEQVKRS PHIRDAVWGS LRSTDSYTVL HYYSNICRLL RFDDGREMYA KFKLRPADPD
VPEDSGKVVP RGILPPETGA IPRDEDDTRP LLFLADDFRR RVGSPDGVRY VFQLQLREVP
TDAAARDVAL DCTRPWDEAE FPYIDVGEVS IGCNLPTEET EKLEFNPFLR CPEVDVIPAT
SCAQSASIDH GRSLVYEICQ RLRNGEPLPA SWRAFLEQSD TKIDLSGCPV AAAATPTRSN
AGDATKVTLA RTWYQALWAT LCQPLLQTLV PYSVLGLVIF LPLRGLLAVA AATRFPLYWL
LPAFWAASGV AAMATCAAAK WALVGSRVDG DTAHIWSPAV FLDTVWQAVR AATAEYFAEL
TPGSAPFAAW MRVMGASVSP GDGVYVDSMG ALLNPEMVRL ERGAAVGRDA LLFGHVYEGE
AGKVKFGAVS VGEDGFVGSR AVAMPSVTVD DGGCLAALGL AMKGETVKHS M
//
