ID   LPXZ_BACTN              Reviewed;         461 AA.
AC   Q8A015;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=BT_4206;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO79311.1; -; Genomic_DNA.
DR   RefSeq; NP_813117.1; NC_004663.1.
DR   RefSeq; WP_008759880.1; NZ_UYXG01000012.1.
DR   AlphaFoldDB; Q8A015; -.
DR   SMR; Q8A015; -.
DR   STRING; 226186.BT_4206; -.
DR   PaxDb; Q8A015; -.
DR   PRIDE; Q8A015; -.
DR   EnsemblBacteria; AAO79311; AAO79311; BT_4206.
DR   GeneID; 60925379; -.
DR   KEGG; bth:BT_4206; -.
DR   PATRIC; fig|226186.12.peg.4273; -.
DR   eggNOG; COG0764; Bacteria.
DR   eggNOG; COG0774; Bacteria.
DR   HOGENOM; CLU_046528_2_0_10; -.
DR   InParanoid; Q8A015; -.
DR   OMA; RRGICHM; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000001414; 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; PTHR30272; PTHR30272; 1.
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..461
FT                   /note="Bifunctional enzyme LpxC/FabZ"
FT                   /id="PRO_0000191975"
FT   REGION          1..302
FT                   /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT   REGION          303..461
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
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"
SQ   SEQUENCE   461 AA;  51600 MW;  633203F800223366 CRC64;
     MLKQKTLKDS FSLSGKGLHT GLDLTVTFNP APDNHGYKIQ RIDLEGQPTI DAVADNVTET
     TRGTVLSKNG VKVSTVEHGM AALYALGIDN CLIQVNGPEF PILDGSAQYY VQEIERVGTE
     EQSAVKDFYI IKSKIEFRDE STGSSIIVLP DENFSLNVLV SYDSTIIPNQ FATLEDMHNF
     KDEVAASRTF VFVREIEPLL SAGLIKGGDL DNAIVIYERK MSQESYDKLA DVMGVPHMDA
     DQLGYINHKP LVWPNECARH KLLDVIGDLA LIGKPIKGRI IATRPGHTIN NKFARQMRKE
     IRLHEIQAPT YDCNREPVMD VNRIRELLPH RYPFQLVDKV IEMGASYIVG IKNITANEPF
     FQGHFPQEPV MPGVLQIEAM AQVGGLLVLN SVDEPERYST YFMKIDGVKF RQKVVPGDTL
     LFRVELLAPI RRGISTMKGY AFVGEKVVCE AEFMAQIVKN K