ID U6RR58_9BACE Unreviewed; 461 AA. AC U6RR58; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 31-JAN-2018, entry version 38. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00388, 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}; 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}; GN Name=fabZ {ECO:0000256|HAMAP-Rule:MF_00406}; GN Synonyms=lpxC {ECO:0000256|HAMAP-Rule:MF_00388}; GN ORFNames=HMPREF1534_00240 {ECO:0000313|EMBL:EOA58276.1}; OS Bacteroides massiliensis B84634 = Timone 84634 = DSM 17679 = JCM OS 13223. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1121098 {ECO:0000313|EMBL:EOA58276.1, ECO:0000313|Proteomes:UP000017831}; RN [1] {ECO:0000313|EMBL:EOA58276.1, ECO:0000313|Proteomes:UP000017831} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B84634 / Timone 84634 / DSM 17679 / JCM 13223 RC {ECO:0000313|Proteomes:UP000017831}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Fenner L., RA Roux V., Mallet M.N., Raoult D., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides massiliensis DSM 17679."; RL Submitted (APR-2013) 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 CC acetate, the committed step in lipid A biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00388, ECO:0000256|SAAS:SAAS00531485}. CC -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. CC Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and CC long chain saturated and unsaturated beta-hydroxyacyl-ACPs. CC {ECO:0000256|HAMAP-Rule:MF_00406, ECO:0000256|SAAS:SAAS00064865}. CC -!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] = CC a trans-2-enoyl-[acyl-carrier protein] + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_00406, ECO:0000256|SAAS:SAAS00371036}. CC -!- CATALYTIC ACTIVITY: UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N- CC acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3- CC hydroxytetradecanoyl)-alpha-D-glucosamine + acetate. CC {ECO:0000256|HAMAP-Rule:MF_00388, ECO:0000256|SAAS:SAAS00531490}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00388, ECO:0000256|SAAS:SAAS00531487}; CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000256|HAMAP- CC Rule:MF_00388, ECO:0000256|SAAS:SAAS00089518}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00406, CC ECO:0000256|SAAS:SAAS00371052}. 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 ECO:0000256|SAAS:SAAS00829032}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOA58276.1}. 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; AQHY01000004; EOA58276.1; -; Genomic_DNA. DR RefSeq; WP_005935988.1; NZ_KB905472.1. DR EnsemblBacteria; EOA58276; EOA58276; HMPREF1534_00240. DR PATRIC; fig|1121098.3.peg.240; -. DR OrthoDB; POG091H0292; -. DR UniPathway; UPA00359; UER00478. DR Proteomes; UP000017831; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047451; F:3-hydroxyoctanoyl-[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 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 Complete proteome {ECO:0000313|Proteomes:UP000017831}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00406, KW ECO:0000256|SAAS:SAAS00448527}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00388, KW ECO:0000256|SAAS:SAAS00041385}; KW Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00406, KW ECO:0000256|SAAS:SAAS00448519}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00406, KW ECO:0000256|SAAS:SAAS00064833}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00406, KW ECO:0000256|SAAS:SAAS00064868}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00406, KW ECO:0000256|SAAS:SAAS00064841}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00388, KW ECO:0000256|SAAS:SAAS00531484}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00388, ECO:0000256|SAAS:SAAS00531488}. FT DOMAIN 328 452 FabA. {ECO:0000259|Pfam:PF07977}. FT ACT_SITE 287 287 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00388}. FT ACT_SITE 364 364 {ECO:0000256|HAMAP-Rule:MF_00406}. FT METAL 78 78 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00388}. FT METAL 260 260 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00388}. FT METAL 264 264 Zinc. {ECO:0000256|HAMAP-Rule:MF_00388}. SQ SEQUENCE 461 AA; 51171 MW; 827284C4891F2622 CRC64; MLKQKTLRGS FSLNGKGLHT GVNLTVTFNP APDNHGYKIQ RIDLEGQPII DAVAENVGDT TRGTVLIKNG IKVSTVEHAL AALYAAGIDN CLIQVNGPEF PILDGSAKQY VECIQRVGIE EQNAVKDYYI IKSKIEFRDE ASGSSIIVLP DENFSVNVLI SYQSKILSNQ FATLEDMSKF PTEVASARTF VFVREIEPLL GAGLIKGGDL DNAIVIYEKE MSQDNYDKLA DVMGVPHMDA TQLGYINHIP LVWDNEPARH KLLDIIGDLA LIGKPIKGRI IATRPGHTIN NKFARQIRKE IKLHEIQAPG YNCNEAPIMD VNRIRELLPH RYPFQLVDKV IAIGANYIVG VKNVTANEPF FQGHFPQEPV MPGVLQIEAM AQCGGLLVLN SVDEPERYST YFLKIDGVKF RQKVVPGDTL IFRVELLAPI RRGVSTMKGY VFVGEKVVCE AEFMAQIVKN K //