LPXC_GLOC7
ID LPXC_GLOC7 Reviewed; 293 AA.
AC B7KKQ2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
DE Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
DE EC=3.5.1.108 {ECO:0000255|HAMAP-Rule:MF_00388};
DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
GN Name=lpxC {ECO:0000255|HAMAP-Rule:MF_00388};
GN OrderedLocusNames=PCC7424_2607;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-
CC acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the
CC committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00388}.
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:0000255|HAMAP-Rule:MF_00388};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388};
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:0000255|HAMAP-
CC Rule:MF_00388}.
CC -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000255|HAMAP-
CC Rule:MF_00388}.
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DR EMBL; CP001291; ACK71021.1; -; Genomic_DNA.
DR RefSeq; WP_015954624.1; NC_011729.1.
DR AlphaFoldDB; B7KKQ2; -.
DR SMR; B7KKQ2; -.
DR STRING; 65393.PCC7424_2607; -.
DR EnsemblBacteria; ACK71021; ACK71021; PCC7424_2607.
DR KEGG; cyc:PCC7424_2607; -.
DR eggNOG; COG0774; Bacteria.
DR HOGENOM; CLU_046528_0_0_3; -.
DR OMA; IVFYRSD; -.
DR OrthoDB; 428602at2; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000002384; Chromosome.
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; IEA:UniProtKB-UniRule.
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-UniRule.
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 3: Inferred from homology;
KW Hydrolase; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..293
FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT /id="PRO_1000122777"
FT ACT_SITE 262
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
SQ SEQUENCE 293 AA; 31930 MW; B285D2A982756FDF CRC64;
MRSHTIKKPF ERSGVGLHSG ITTQVKVLPA KPGEGRYFVR VDLPQQPIIP AKLAYVNQTP
LSTELKSPQG SVRTVEHLLA ALSGSGINDV RIEIDGPEVP LLDGSAQQWI EAIASAGMIE
LTDEETTPTV MISSPISVQE GDAFVLALPA RELRFTYGID FAYSVIGNQW YSWNPASESF
AEAIAPARTF GFADQIESLK QAGLIKGGSL ENALVCDHQG WVNPPLRFSN EPVRHKLLDL
VGDLSLLETI PLAHFLAYKA SHKLHIELAK AIHGTVKVSE HHFKGFPENA LTS
