ID   A0A416VJ64_9BACE        Unreviewed;       461 AA.
AC   A0A416VJ64;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   05-JUN-2019, entry version 2.
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.
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
RT   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
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:SAAS00371087}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-
CC         alpha-D-glucosamine = acetate + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-alpha-D-glucosamine; Xref=Rhea:RHEA:25209,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:61494,
CC         ChEBI:CHEBI:71573; EC=3.5.1.108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00388, ECO:0000256|SAAS:SAAS01120543};
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;
CC         EC=4.2.1.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00406,
CC         ECO:0000256|SAAS:SAAS01122688};
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:SAAS00041382}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00406,
CC       ECO:0000256|SAAS:SAAS00064863}.
CC   -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00388, ECO:0000256|SAAS:SAAS00904468}.
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:RHR69940.1}.
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DR   EMBL; QUHA01000038; RHR69940.1; -; Genomic_DNA.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000283562; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000283562};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00406,
KW   ECO:0000256|SAAS:SAAS00064829};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00436291};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00064858};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00448566};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00448576};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00406,
KW   ECO:0000256|SAAS:SAAS00448581};
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;  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
//