FAAH_ORYSI
ID FAAH_ORYSI Reviewed; 608 AA.
AC Q01N44; B8ATY3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Fatty acid amide hydrolase {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q0JFH7};
DE AltName: Full=N-acylethanolamine amidohydrolase {ECO:0000305};
GN Name=FAAH {ECO:0000305};
GN ORFNames=OSIGBa0123D13.5 {ECO:0000312|EMBL:CAH65756.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of bioactive endogenous fatty acid
CC amides to their corresponding acids. The hydrolysis of endogenous
CC amidated lipids terminates their participation as lipid mediators in
CC various signaling systems. Converts a wide range of N-acylethanolamines
CC (NAEs) to their corresponding free fatty acids and ethanolamine.
CC {ECO:0000250|UniProtKB:Q0JFH7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z,12Z-octadecadienoyl)-ethanolamine = (9Z,12Z)-
CC octadecadienoate + ethanolamine; Xref=Rhea:RHEA:35567,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30245, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:64032; Evidence={ECO:0000250|UniProtKB:Q0JFH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35568;
CC Evidence={ECO:0000250|UniProtKB:Q0JFH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine +
CC hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464;
CC Evidence={ECO:0000250|UniProtKB:Q0JFH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065;
CC Evidence={ECO:0000250|UniProtKB:Q0JFH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine;
CC Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:85263;
CC Evidence={ECO:0000250|UniProtKB:Q0JFH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457;
CC Evidence={ECO:0000250|UniProtKB:Q0JFH7};
CC -!- ACTIVITY REGULATION: Inhibited by methyl arachidonyl fluorophosphonate
CC (MAFP). {ECO:0000250|UniProtKB:Q0JFH7}.
CC -!- SUBUNIT: Forms homodimers. {ECO:0000250|UniProtKB:Q7XJJ7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q7XJJ7}. Cell membrane
CC {ECO:0000250|UniProtKB:Q7XJJ7}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC76621.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR854996; CAH65756.1; -; Genomic_DNA.
DR EMBL; CM000129; EEC76621.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q01N44; -.
DR SMR; Q01N44; -.
DR STRING; 39946.B8ATY3; -.
DR EnsemblPlants; BGIOSGA015740-TA; BGIOSGA015740-PA; BGIOSGA015740.
DR Gramene; BGIOSGA015740-TA; BGIOSGA015740-PA; BGIOSGA015740.
DR HOGENOM; CLU_009600_0_2_1; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Cell membrane; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..608
FT /note="Fatty acid amide hydrolase"
FT /id="PRO_0000451043"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT ACT_SITE 306
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT BINDING 303..306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
SQ SEQUENCE 608 AA; 66547 MW; 9CE942BAA8E13ED8 CRC64;
MGKPPRAMTP VEEVDLSAVR YQSPSLQAPH LTGFSLRAFV WLMESPLFGR LLTSVLKSQN
NITRMLQDTV IPERPMYLPE YPPQEPEQGV LLLGDDRDPV DRVEEALHCL PPYDPSLRWP
AGDKPPFLYW KIRDFAHAYR SGITTPSVVA EHIIAGVEEW SNKKPPMPML VYFNADDLRK
QAEASTKRFQ QGNPISILDG IFIAIKDDID CFPYPSKGAT TFFDKIRSVE KDAVCVARLR
KCGVLFIGKA NMHELGLGVT GNNPNYGTAR NPHSIDRYTG GSSSGPAALV SSGLCSAAIG
TDGGGSVRIP SSLCGIIGLK TTYGRTDMTG ALCDCGTVEV ASPLAASVED ALLVYSAIAG
SRPMDKLTLR PSPLCVPNLV SPDNNNILGS VKIGKYTEWF HDVSDRDISN TCEDALNLLC
SSFGCQIEEI ILPELEEMRT AHVVSIGTES FCDLNPHYRA GKRTEFTLDT RTSLALFGSF
TSTDYVASQR IRRRIMYYHN EAFKKVDVIA TPTTGITAPE IPQSSLKLGE SNYVVSAYLM
RFVIAGNLLG LPAITVPVGH DKQGLPIGLQ LIGRPWGEAS LLRVASAIEE LCLKKRKRPS
AFHDILNA
