ID A0A416VJ64_9BACE Unreviewed; 461 AA. AC A0A416VJ64; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 02-JUN-2021, entry version 9. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00388, ECO:0000256|HAMAP-Rule:MF_00406}; DE Includes: DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000256|HAMAP-Rule:MF_00406}; DE EC=4.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00406}; DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000256|HAMAP-Rule:MF_00406}; DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000256|HAMAP-Rule:MF_00406}; DE Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000256|HAMAP-Rule:MF_00406}; DE Includes: DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000256|HAMAP-Rule:MF_00388}; DE Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000256|HAMAP-Rule:MF_00388}; DE EC=3.5.1.108 {ECO:0000256|HAMAP-Rule:MF_00388}; DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000256|HAMAP-Rule:MF_00388}; GN Name=lpxC {ECO:0000256|HAMAP-Rule:MF_00388}; GN Synonyms=fabZ {ECO:0000256|HAMAP-Rule:MF_00406}; GN ORFNames=DWW69_18610 {ECO:0000313|EMBL:RHR69940.1}; OS Bacteroides sp. AF16-49. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; unclassified Bacteroides. OX NCBI_TaxID=2292192 {ECO:0000313|EMBL:RHR69940.1, ECO:0000313|Proteomes:UP000283562}; RN [1] {ECO:0000313|EMBL:RHR69940.1, ECO:0000313|Proteomes:UP000283562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16-49 {ECO:0000313|EMBL:RHR69940.1, RC ECO:0000313|Proteomes:UP000283562}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00002923, CC ECO:0000256|HAMAP-Rule:MF_00388}. 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:0000256|HAMAP- CC Rule:MF_00406}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D- CC glucosamine = acetate + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha- CC D-glucosamine; Xref=Rhea:RHEA:25209, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:61494, ChEBI:CHEBI:71573; CC EC=3.5.1.108; Evidence={ECO:0000256|ARBA:ARBA00000468, CC ECO:0000256|HAMAP-Rule:MF_00388}; 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 Evidence={ECO:0000256|HAMAP-Rule:MF_00406}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947, CC ECO:0000256|HAMAP-Rule:MF_00388}; CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000256|ARBA:ARBA00004934}. 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 ECO:0000256|HAMAP-Rule:MF_00388}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00406}. CC -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000256|HAMAP- CC Rule:MF_00388}. CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00406}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RHR69940.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QUHA01000038; RHR69940.1; -; Genomic_DNA. DR UniPathway; UPA00359; UER00478. DR Proteomes; UP000283562; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00406}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00388}; KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00406}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00388}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00388}. FT ACT_SITE 287 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" FT ACT_SITE 364 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00406" FT METAL 78 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" FT METAL 260 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" FT METAL 264 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388" SQ SEQUENCE 461 AA; 51601 MW; 47493D757C558F0F CRC64; MLKQKTLKDS FSLRGKGLHT GLDITITFNP AAENHGYKIQ RIDLEGQPII DAVADNVVET TRGTVLAKND VKVSTVEHAM AALYAAGIDN CLIQVNGPEF PILDGSAIYY VEGIEKVGIE EQTAVKDYYI IKSKIEFKDE KTGSSIIVLP DDSFSVNALI SYDSKIIPNQ FATLEDMNDF PKEIAGSRTF VFVREIEPLL GAGLIKGGDL DNAIVIYERQ MSQENFDKLA DVMGVPHMNA NQMGYINHKP LVWDNEPARH KLLDIIGDLA LIGRPIKGRI IATRPGHTIN NKFARQMRKE IRLHEIQAPI YNCSEEPVMD INRIRELLPH RYPFLLVDKI IEIGPNHIVG VKNVTTNEPF FQGHFPQEPV MPGVLQVEAM AQVGGLLVLN SVDEPERYST YFMKIDGVKF RQKVVPGDTL LFRLELLAPI RRGISTMKGY VFVGEKVACE AEFMAQIIKN K //