ID A0A0S7BWY6_9BACT Unreviewed; 466 AA.
AC A0A0S7BWY6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=TBC1_111257 {ECO:0000313|EMBL:GAP43115.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP43115.1};
RN [1] {ECO:0000313|EMBL:GAP43115.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP43115.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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.
CC {ECO:0000256|ARBA:ARBA00025049, ECO:0000256|HAMAP-Rule:MF_00406}.
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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00024535, ECO:0000256|HAMAP-
CC Rule:MF_00388};
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; 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}.
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DR EMBL; DF968182; GAP43115.1; -; Genomic_DNA.
DR RefSeq; WP_062039868.1; NZ_DF968182.1.
DR AlphaFoldDB; A0A0S7BWY6; -.
DR STRING; 1678841.TBC1_111257; -.
DR PATRIC; fig|1678841.3.peg.1426; -.
DR OrthoDB; 9772788at2; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[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 CDD; cd01288; FabZ; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.30.230.20; lpxc deacetylase, domain 1; 1.
DR Gene3D; 3.30.1700.10; lpxc deacetylase, domain 2; 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_Su5_D2-typ_SF.
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 NCBIfam; TIGR01750; fabZ; 1.
DR NCBIfam; TIGR00325; lpxC; 1.
DR PANTHER; PTHR33694; UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR33694:SF1; UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07977; FabA; 1.
DR Pfam; PF03331; LpxC; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00388}.
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
FT ACT_SITE 367
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
SQ SEQUENCE 466 AA; 52425 MW; C50F72AFBA692ADF CRC64;
MSEKQKTLKE AVTISGAGLH TGREVNLTFR PAPENHGFKF RRTDLPGQPV IDADADLVTD
TSRGTTIEHN GVRVSTIEHA LAALTGMDLD NILIDLDCPE TPILDGSSKF YIEGIKKAGV
VEQNAERQYF RINEVLRYSD PEKKTELLIL PDDTYKVSVM IDYDTKVLGT QNAHLSHLND
FAEEISPCRT FVFLHELELL IQNNLIKGGD LSNAIVFVNR LISQEELDRL AKFFNKPRVE
VLKEGILNNL ELYFNNEPAR HKLLDVVGDL SLVGTRIKGH VIASRPGHLA NTHFARIIKQ
HIKHETSQPQ QPKFDPGKPP LYDINDIKRL LPHRPPFLLV DKILEMSDHD VTGLKNVTMN
EGFFVGHFPD EPVMPGVLII EAMAQAGGIF VLSSFPDPEN YITYFMKIDN VRFRQKVVPG
DTLIFHLELM SPFRRGISHM RGVAYVGNKI VAEAELMAQI TKKTVS
//
