FAAH_MEDTR
ID FAAH_MEDTR Reviewed; 607 AA.
AC G7ISB0; Q4FCX5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Fatty acid amide hydrolase {ECO:0000303|PubMed:16624618};
DE EC=3.5.1.- {ECO:0000269|PubMed:16624618};
DE AltName: Full=N-acylethanolamine amidohydrolase {ECO:0000303|PubMed:16624618};
GN Name=FAAH {ECO:0000303|PubMed:16624618};
GN OrderedLocusNames=MTR_2g010180 {ECO:0000312|EMBL:AES63571.2};
GN ORFNames=MtrunA17_Chr2g0279961 {ECO:0000312|EMBL:RHN71727.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16624618; DOI=10.1016/j.bbalip.2006.03.004;
RA Shrestha R., Kim S.C., Dyer J.M., Dixon R.A., Chapman K.D.;
RT "Plant fatty acid (ethanol) amide hydrolases.";
RL Biochim. Biophys. Acta 1761:324-334(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
CC -!- FUNCTION: Catalyzes the hydrolysis of bioactive endogenous fatty acid
CC amides to their corresponding acids (PubMed:16624618). The hydrolysis
CC of endogenous amidated lipids terminates their participation as lipid
CC mediators in various signaling systems (Probable). Converts a wide
CC range of N-acylethanolamines (NAEs) to their corresponding free fatty
CC acids and ethanolamine (PubMed:16624618). {ECO:0000269|PubMed:16624618,
CC ECO:0000305|PubMed:16624618}.
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:0000269|PubMed:16624618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35568;
CC Evidence={ECO:0000269|PubMed:16624618};
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}.
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DR EMBL; DQ091761; AAZ04133.1; -; mRNA.
DR EMBL; CM001218; AES63571.2; -; Genomic_DNA.
DR EMBL; PSQE01000002; RHN71727.1; -; Genomic_DNA.
DR RefSeq; XP_003593320.2; XM_003593272.2.
DR AlphaFoldDB; G7ISB0; -.
DR SMR; G7ISB0; -.
DR STRING; 3880.AES63571; -.
DR EnsemblPlants; AES63571; AES63571; MTR_2g010180.
DR GeneID; 11429245; -.
DR Gramene; AES63571; AES63571; MTR_2g010180.
DR Proteomes; UP000002051; Chromosome 2.
DR Proteomes; UP000265566; Chromosome 2.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047412; F:N-(long-chain-acyl)ethanolamine deacylase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..607
FT /note="Fatty acid amide hydrolase"
FT /id="PRO_0000451044"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT ACT_SITE 304
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT BINDING 301..304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT CONFLICT 303
FT /note="G -> S (in Ref. 1; AAZ04133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 66177 MW; 7819DA4BA135376C CRC64;
MGKKRVMVPA KDVDLSSIKY EPEIVQAPHL TGFWFRFFVR LIEAPLIGPF LLTMLKKENK
IDQLLRNTVF PEEPMFKPEY PPQEKEHSVV ELDEDGRPEG RVESALNCLP HYDPAKLWEN
SSATFRYWKI RDYAYAYQSR KVTPSMVAES IISMIEENGI DKPPTPLLLS FDAAEVRKQA
AASTQRFESG NPLSILDGIF IAIKDDIDCH PHPSTGGSTW MHEVRDVKKD AVCVSRLRSC
GVIFIGKTNM HEFGMGTTGN NSNYGTARNP HAPDRYTGGS SSGPAAIVAS GLCSAALGTD
GGGSVRIPSS LCGVVGLKIN YGRTSMEGSL CDSGTVEVIG PIASTVEDAM LVYAAMLGAS
PANRISMKPS TPCLPTLSSD DDTDALRSLR IGIYTPWFNN VHSTEVSDKC EDALNLLSKA
HGCEVVEVVI PEIVEMRTAH LVSIGSECLS SLNPDIEDGK GVKLSYDTRT SLALFQSFTA
ADYVAAQCIR RRIMHYFMEI FKKVDVIVTP TTGMTAPRIP PSALKSGETD MPTTGYLMRF
VVPANLLGLP AISVPVGYDK EGLPIGLQVI GRPWAEATIL RVAAAVEKLC GESKRRPVTY
YDVLGAN
