LPXZ_CHLTE
ID LPXZ_CHLTE Reviewed; 467 AA.
AC Q8KBX0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Bifunctional enzyme LpxC/FabZ;
DE Includes:
DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase;
DE Short=UDP-3-O-acyl-GlcNAc deacetylase;
DE EC=3.5.1.108;
DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase;
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ;
DE EC=4.2.1.59;
DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase;
DE Short=(3R)-hydroxymyristoyl-ACP dehydrase;
DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase;
GN Name=lpxC/fabZ; OrderedLocusNames=CT1662;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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.
CC -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes
CC the dehydration of short chain beta-hydroxyacyl-ACPs and long chain
CC saturated and unsaturated beta-hydroxyacyl-ACPs. {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the LpxC family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the thioester
CC dehydratase family. {ECO:0000305}.
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DR EMBL; AE006470; AAM72887.1; -; Genomic_DNA.
DR RefSeq; NP_662545.1; NC_002932.3.
DR RefSeq; WP_010933326.1; NC_002932.3.
DR STRING; 194439.CT1662; -.
DR EnsemblBacteria; AAM72887; AAM72887; CT1662.
DR KEGG; cte:CT1662; -.
DR PATRIC; fig|194439.7.peg.1500; -.
DR eggNOG; COG0764; Bacteria.
DR eggNOG; COG0774; Bacteria.
DR HOGENOM; CLU_046528_2_0_10; -.
DR OMA; RRGICHM; -.
DR OrthoDB; 231861at2; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
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_00406; FabZ; 1.
DR HAMAP; MF_00388; LpxC; 1.
DR InterPro; IPR013114; FabA_FabZ.
DR InterPro; IPR010084; FabZ.
DR InterPro; IPR029069; HotDog_dom_sf.
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; 2.
DR Pfam; PF07977; FabA; 1.
DR Pfam; PF03331; LpxC; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR01750; fabZ; 1.
DR TIGRFAMs; TIGR00325; lpxC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Metal-binding; Multifunctional enzyme;
KW Reference proteome; Zinc.
FT CHAIN 1..467
FT /note="Bifunctional enzyme LpxC/FabZ"
FT /id="PRO_0000191974"
FT REGION 1..306
FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT REGION 307..467
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase"
FT ACT_SITE 291
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 370
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 51844 MW; 355120C7D2B654E7 CRC64;
MLIHQRTLQN EISLTGIGLH TGHECTITFK PAPVNTGYIF VRTDINDCPE IPALIDHVVD
VLRGTTIGIG DVKVHTTEHV LAALYGLQID NCRIELSGPE PPVLDGSSNP FAEALLSAGI
AEQDEPKNYL VIDETIEFHN PEKSVDIVAL PLDGFRMTVM VDYKNPALGS QHSGLFDLDK
EFLREFSPCR TFCFLSEVEA MANQGIIKGA DIDNAIVIVD KQLDETEVQT LADKVGVDAS
HLVLGQNGIL NNRELRFSNE PARHKLLDLL GDLALLGMPV KAQILAXRPG HASNVEFVKQ
LKKYADRNKL ARQYQHEKKA GVIFDINAIQ NILPHRYPFL LIDKIVEFKL DEKIVSIKNV
TMNEPFFQGH FPGNPIMPGV LIIEAMAQTG GIMMLNGKEN IKESVVFFMG IDKARFRKPV
LPGDTLVIEA VMTNMRRTVC QFDAKAYVRG ELVCEASLMA TVMEKKN
