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LPXC5_ARATH
ID   LPXC5_ARATH             Reviewed;         326 AA.
AC   F4IAW1; B3H6R1; P0C2G7; Q56X64; Q56XG5; Q7GAV1; Q8GXP0; Q8LPR6; Q9FE36;
AC   Q9FXK3; Q9FXK7;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 5, mitochondrial {ECO:0000250|UniProtKB:P0A725};
DE            Short=UDP-3-O-acyl-GlcNAc deacetylase 5 {ECO:0000250|UniProtKB:P0A725};
DE            EC=3.5.1.108 {ECO:0000250|UniProtKB:P0A725};
DE   AltName: Full=Protein LIPID X C5;
DE            Short=AtLpxC5;
DE   AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase 5 {ECO:0000250|UniProtKB:P0A725};
DE   Flags: Precursor;
GN   Name=LPXC5; OrderedLocusNames=At1g25210; ORFNames=F4F7.44;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   PATHWAY, SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=21709257; DOI=10.1073/pnas.1108840108;
RA   Li C., Guan Z., Liu D., Raetz C.R.;
RT   "Pathway for lipid A biosynthesis in Arabidopsis thaliana resembling that
RT   of Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:11387-11392(2011).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   TYR-21.
RX   PubMed=25732537; DOI=10.1093/jxb/erv064;
RA   Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT   "Identification of cleavage sites and substrate proteins for two
RT   mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL   J. Exp. Bot. 66:2691-2708(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC       glycolipid that in bacteria anchors the lipopolysaccharide to the outer
CC       membrane of the cell. Lipid A-like molecules in plants may serve as
CC       structural components of the outer membranes of mitochondria and/or
CC       chloroplasts, or may be involved in signal transduction or plant
CC       defense responses (Potential). {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine +
CC         H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate;
CC         Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108;
CC         Evidence={ECO:0000250|UniProtKB:P0A725};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0A725};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC       from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC       acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000269|PubMed:21709257}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21709257,
CC       ECO:0000305|PubMed:25732537}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=F4IAW1-1; Sequence=Displayed;
CC   -!- MISCELLANEOUS: Plants silencing LPXC do not have altered morphology
CC       compared to wild-type plants when grown under normal growth conditions,
CC       but they do not accumulate 2,3-diacylglucosamine-1-phosphate.
CC       {ECO:0000305|PubMed:21709257}.
CC   -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG28816.2; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g25210 and At1g25211.; Evidence={ECO:0000305};
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DR   EMBL; AC079374; AAG28816.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30587.2; -; Genomic_DNA.
DR   RefSeq; NP_001117349.4; NM_001123877.5. [F4IAW1-1]
DR   RefSeq; NP_001185090.1; NM_001198161.1. [F4IAW1-1]
DR   RefSeq; NP_173874.2; NM_102312.3. [F4IAW1-1]
DR   RefSeq; NP_849706.4; NM_179375.4. [F4IAW1-1]
DR   AlphaFoldDB; F4IAW1; -.
DR   SMR; F4IAW1; -.
DR   PRIDE; F4IAW1; -.
DR   EnsemblPlants; AT1G24793.1; AT1G24793.1; AT1G24793.
DR   EnsemblPlants; AT1G25054.1; AT1G25054.1; AT1G25054.
DR   EnsemblPlants; AT1G25145.1; AT1G25145.1; AT1G25145.
DR   EnsemblPlants; AT1G25210.2; AT1G25210.2; AT1G25210.
DR   GeneID; 10723064; -.
DR   GeneID; 839084; -.
DR   GeneID; 839094; -.
DR   GeneID; 839102; -.
DR   Gramene; AT1G24793.1; AT1G24793.1; AT1G24793.
DR   Gramene; AT1G25054.1; AT1G25054.1; AT1G25054.
DR   Gramene; AT1G25145.1; AT1G25145.1; AT1G25145.
DR   Gramene; AT1G25210.2; AT1G25210.2; AT1G25210.
DR   KEGG; ath:AT1G24793; -.
DR   KEGG; ath:AT1G25054; -.
DR   KEGG; ath:AT1G25145; -.
DR   KEGG; ath:AT1G25210; -.
DR   Araport; AT1G25210; -.
DR   TAIR; locus:1005716744; AT1G25210.
DR   HOGENOM; CLU_046528_0_0_1; -.
DR   OMA; IVFYRSD; -.
DR   PhylomeDB; F4IAW1; -.
DR   UniPathway; UPA00359; UER00478.
DR   PRO; PR:F4IAW1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IMP:UniProtKB.
DR   GO; GO:0103117; F:UDP-3-O-acyl-N-acetylglucosamine deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001289; P:lipid X metabolic process; IMP:UniProtKB.
DR   Gene3D; 3.30.1700.10; -; 1.
DR   Gene3D; 3.30.230.20; -; 1.
DR   HAMAP; MF_00388; LpxC; 1.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR004463; UDP-acyl_GlcNac_deAcase.
DR   InterPro; IPR011334; UDP-acyl_GlcNac_deAcase_C.
DR   InterPro; IPR015870; UDP-acyl_N-AcGlcN_deAcase_N.
DR   PANTHER; PTHR33694; PTHR33694; 1.
DR   Pfam; PF03331; LpxC; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   TIGRFAMs; TIGR00325; lpxC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Metal-binding; Mitochondrion; Reference proteome;
KW   Transit peptide; Zinc.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           22..326
FT                   /note="Probable UDP-3-O-acyl-N-acetylglucosamine
FT                   deacetylase 5, mitochondrial"
FT                   /id="PRO_0000419661"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A725"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A725"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A725"
SQ   SEQUENCE   326 AA;  35717 MW;  CBF391A5DFB4EEA9 CRC64;
     MRLPVTVKAT KPSFLVIWIR YSSAASSPTV SLNPSGRLQQ TLAGSVEVKG KSLHSGKFST
     VKLNPEIAGA GRFFEFRSRF IPASIEFAQE SPLCTTLLKD ELKIRTVEHL LSALEAKGVD
     NCRIQIESES SDDREVEVPI FDGSAKEWVD AIQGVGINAA QNHDGESVEK MVAHVNKPVY
     VCKNDTFVAA FPALETRITC GIDFPQVPAI GCQWFSWRPI HESSFAKDIA SSRTFCVYEE
     VERMREAGLI KGGSLDNAIV CSAEHGWMNP PLRFDDEACR HKILDLIGDL SLVSRGGNGG
     LPVAHIVAYK AGHALHTDLA RHLTMD
 
 
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