ID A0A0D9VRE4_9ORYZ Unreviewed; 1569 AA.
AC A0A0D9VRE4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00012745};
DE EC=3.5.1.108 {ECO:0000256|ARBA:ARBA00012745};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR03G08030.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR03G08030.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR03G08030.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR03G08030.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00024987}.
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:0000256|ARBA:ARBA00024535};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:0000256|ARBA:ARBA00005002}.
CC -!- SIMILARITY: Belongs to the LpxC family.
CC {ECO:0000256|ARBA:ARBA00006170}.
CC -!- SIMILARITY: Belongs to the non-repetitive/WGA-negative nucleoporin
CC family. {ECO:0000256|ARBA:ARBA00007373}.
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DR EnsemblPlants; LPERR03G08030.1; LPERR03G08030.1; LPERR03G08030.
DR Gramene; LPERR03G08030.1; LPERR03G08030.1; LPERR03G08030.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000032180; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0005643; C:nuclear pore; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IEA:UniProtKB-EC.
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; IEA:UniProt.
DR Gene3D; 1.20.58.1780; -; 1.
DR Gene3D; 3.30.230.20; lpxc deacetylase, domain 1; 1.
DR Gene3D; 3.30.1700.10; lpxc deacetylase, domain 2; 1.
DR Gene3D; 1.25.40.450; Nucleoporin, helical domain, N-terminal subdomain; 1.
DR HAMAP; MF_00388; LpxC; 1.
DR InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR InterPro; IPR004870; Nucleoporin_Nup155.
DR InterPro; IPR042533; Nucleoporin_Nup155_C_1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
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 NCBIfam; TIGR00325; lpxC; 1.
DR PANTHER; PTHR10350; NUCLEAR PORE COMPLEX PROTEIN NUP155; 1.
DR PANTHER; PTHR10350:SF6; NUCLEAR PORE COMPLEX PROTEIN NUP155; 1.
DR Pfam; PF03331; LpxC; 1.
DR Pfam; PF08801; Nucleoporin_N; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 55..497
FT /note="Nucleoporin Nup133/Nup155-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08801"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1569 AA; 170284 MW; 7119F8CFA67A45DB CRC64;
MAWAEDEAIG PDVASAGQHV SERIGRDAAA QPDLEEALEA SRYASHPYSS HPKEWPPLVE
VAETRQLPPI LVERYNAVAG EGTALCGIFS EIHRAWATVD NSFFIWRFDK WDGQCQEYNA
NEQVICAVGL ARAKPGIFVE AIQYLLVLAT PIELMLVGVC CSASGDGTNP YAELSLQPLP
EYMISTDGVT VTCITCTDKG QIFLAGRDGH IYELQYTTGS GWRKRCRKVC LTAGLGSLLS
RWVLPNAFKF SAVDPIVDMV IDEERNTIYA RTEGMKLQLF DLGASGDGPL KKITEERNLV
DPRDAPYGSR RPNAQRAARS PKPSIVCIAP LSAMESKWLH AVAVLSDGKR LFLSTSGGSS
SVGLSTGLQR PSCLKIVATR PSPPLGVGGG LTFGAVSAAG RAQPEDLALK VESAFYSAGA
LIMSDSSATA MSSLLAVQKD SAAQLSLPST FGTASRSSRA LRETVSALPV EGRMLCASDV
FPPPDAAFIM QSLYADVECF AAFGKPSEKS SIKLWAKGDL PTQHILPRRR IVVFNTMGLM
EVVFNRPVDI LRKLLDGNTL RSQLEEFFNR FGTGEAAAMC LMLATKLLYT EDSLISNAVS
EKAAEAFEDP ALVGMPQIDG STALSNTRTQ AGGFSMGQVV QEAQPIFSGA YEGLCLCSSR
LLYPIWELPI MVVRGLVGSN DRGDGVVVCR LSTGAMKVLE SKIRSLETFF RSRRNKRRGL
YGYVAGLGDS GSILYKAGPI IGSGGHSSGK SPYSSHIRDV NPTDQSASNK KQRLPCTSAE
LAAMEVRAIE CLRRLLRRSG EALFLLQLIC QHNVARLVQT LGSDLRKKLV QLTFHQLVCS
EDGDQLAMRL ISALMEYYIG PEGTGTIEEI STKLREGCPS YFNESDYKYY LAVECLERAS
VINNYEQKDI LARDAYNLLT KIPDSADLSA ICKRFENLRF YEAVVRLPLQ KAQALDSHAD
VINGQIDGRH HDIITAQREQ CYKIVMNALC TLKGVGQSGT QGADKSSGSV TAIDPVSRGK
YIRQIIQLSV QWPDTMFHEH LYKTLIELGL ENELLEYGGS DLVAFLQSAG RKHHEEERLS
SGEELVGDED VARALLGACK DLPEPVLAVY DQLLSNGAIV PSLNLKLRLL RSVLAILREW
GMSVVAHKLG TTTAGASFFL DGTFSLNQTG SLNKGIRDKI ISLANRYMTE VRRLNLPQSQ
TETVYRGFRE LEEKLLSQTT PNTCWVGKSE VQFPLTAAAA AAVVVMCGAA ARALNSVSRG
AFSWKPTGFP QQTLAAAVSR SGVGLHSGAR TTARLIPARA GEGRYFVVEG EGEGETRVAA
EVANAEARSP LCTTLRRGGA RVRTVEHLLS AMEALGVDNC RVEVSGGDEI PLLDGSAQEW
VEAIRGASLC AAKDSSGQKM EKLAPEINKP VYLQKSDCFV AALPSSRIRI TYGIDFPKVS
AIGCQRFATV LDANVYSNKI APARTFCVFE EVEKLRAAGL IKGGSLENAM VCSTSGGWLN
PPLRFEDEPC RHKSLDLIGD FSLLAQNGNQ GFPIAHVVAY KAGHALHTDF LWHLLGRSIV
GQEKLAVQC
//
