ID A0A286ADL2_9SPHI Unreviewed; 470 AA.
AC A0A286ADL2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=fabZ {ECO:0000256|HAMAP-Rule:MF_00406};
GN Synonyms=lpxC {ECO:0000256|HAMAP-Rule:MF_00388};
GN ORFNames=SAMN06297358_3696 {ECO:0000313|EMBL:SOD19988.1};
OS Pedobacter xixiisoli.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1476464 {ECO:0000313|EMBL:SOD19988.1, ECO:0000313|Proteomes:UP000219281};
RN [1] {ECO:0000313|EMBL:SOD19988.1, ECO:0000313|Proteomes:UP000219281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12803 {ECO:0000313|EMBL:SOD19988.1,
RC ECO:0000313|Proteomes:UP000219281};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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.
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; OCMT01000004; SOD19988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286ADL2; -.
DR OrthoDB; 9772788at2; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000219281; 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; 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};
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 470 AA; 52116 MW; 4EE5B945EAE3F9CC CRC64;
MNVKQRTIKG EISVQGVGLH TGANVTLTFC PAPENHGFKF QRVDLPGEPI IDADCDNVTD
TARGTTITQN GASVSTVEHV MASLVGMDLD NVLVKVDGPE TPIMDGSSIK FIEVLEQVGS
ALQNADREYY TIPHNITYTE PERSVEIVAM PLDDYRFTCM IDYNSPVLGS QHAGITTIGE
FKKEIASCRT FCFLHELEYQ LQHNLIKGGD LNNAIVIVDK EVTKEELQHL AKIFNREEID
VAPQGILNNM ELRYQNEPAR HKLLDMIGDL ALVGVHLKGH IMAARPGHAA NVAFAKKIKA
AIKKEKGKKK LNTYDVNAKP LYDVVDVMKI LPHRQPFLFV DKVLELSKTH VVGVKNVTMN
EEFFKGHFPG APVFPGVIQI EAMAQTGGIL VLSTVPDPEN YLTYFLKIDN VRFRAQVLPG
DTIVFRCDLV EPMRRGIAQM KGVGMVGEKV VVEAEMMAQI VKVKESEITK
//
