LPXZ_PORGI
ID LPXZ_PORGI Reviewed; 462 AA.
AC Q7MXT8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=PG_0071;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(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; AE015924; AAQ65320.1; -; Genomic_DNA.
DR RefSeq; WP_005873963.1; NC_002950.2.
DR AlphaFoldDB; Q7MXT8; -.
DR SMR; Q7MXT8; -.
DR STRING; 242619.PG_0071; -.
DR EnsemblBacteria; AAQ65320; AAQ65320; PG_0071.
DR GeneID; 29257155; -.
DR KEGG; pgi:PG_0071; -.
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; UP000000588; 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.
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..462
FT /note="Bifunctional enzyme LpxC/FabZ"
FT /id="PRO_0000191976"
FT REGION 1..302
FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT REGION 303..462
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 462 AA; 51691 MW; C92043D1C1310DEC CRC64;
MQKQQTLKDK FCLQGKGLHT GLDIHITFCP APEESGYKIK RVDLEGQPVI DAIADNVHST
RRGTVLKKGE VSVSTIEHAM AALYALGVDN CLIEVDAPEF PILDGSAEPY VSEIKRVGLV
EQETPRDYYI IKKRMEVSDP ESNSKLILLP DDEFTVDVHI AFPSKVLSNQ FASLETLSDF
EEQIAGARTF VFVREVQMLL EANLIKGGDL DNALVIYDEP LAQDRLDALS DMMGVERKQV
NELGYINNKP LIYDNEPARH KLLDVLGDLA LIGKYIRGRI IATCPGHSIN NKMARLIRKE
IKQNEAQAPV YNPNKEPIMD INRIKELLPH RYPFLLVDKI IEVGPDYIVG VKSVSGNEPF
FPGHFPGEPV MPGVLQVEAM AQVGGLLVLN TLTEPSSYST YFLMIDKVKF RRKVVPGDTL
VFKLRMISEI RRGVANMRGL AFVGEQLACE AEFMAQIIQN KE
