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Database: UniProt
Entry: A0A0J0YK44_9FLAO
LinkDB: A0A0J0YK44_9FLAO
Original site: A0A0J0YK44_9FLAO 
ID   A0A0J0YK44_9FLAO        Unreviewed;       462 AA.
AC   A0A0J0YK44;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=AB674_06930 {ECO:0000313|EMBL:KLT70536.1};
OS   Flavobacterium sp. ABG.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1423322 {ECO:0000313|EMBL:KLT70536.1, ECO:0000313|Proteomes:UP000036173};
RN   [1] {ECO:0000313|EMBL:KLT70536.1, ECO:0000313|Proteomes:UP000036173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABG {ECO:0000313|EMBL:KLT70536.1,
RC   ECO:0000313|Proteomes:UP000036173};
RA   Gimbel A.B., Miller J.R., Newman J.D.;
RT   "Flavobacterium sp. ABG.";
RL   Submitted (JUN-2015) 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}.
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:KLT70536.1}.
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DR   EMBL; LEKS01000005; KLT70536.1; -; Genomic_DNA.
DR   RefSeq; WP_047775377.1; NZ_LEKS01000005.1.
DR   AlphaFoldDB; A0A0J0YK44; -.
DR   STRING; 1423322.AB674_06930; -.
DR   PATRIC; fig|1423322.9.peg.1476; -.
DR   OrthoDB; 9772788at2; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000036173; 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};
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        365
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
SQ   SEQUENCE   462 AA;  51233 MW;  8371C55A683F802C CRC64;
     MVKQKTIKNE ISLTGVGLHT GKEVTMTFKP APINNGFTFV RVDLQGQPVI EADANYVVNT
     QRGTNLEKLG VKIQTPEHVL AALVGCDLDN VIIELDASEL PIMDGSSKYF VEAIENAGIE
     EQDAKRNVYV VKEVISFTDE ATGSEILVMP SDDYQVTAMV DFGTKVLGTQ NATMKSIADF
     KDEISNSRTF SFLHELESLL ENGLIKGGDL NNAIVYVDKE ISDATMENLK KAFGKDKISV
     KPNGVLDNLT LHYPNEAARH KLLDVVGDLA LIGVRIQGKI IANKPGHYVN TQFAKKIGKI
     IKIEQRNHVP VYDLNKEPLM DIHKIMAMLP HRPPFLLIDR IIEMSDRHVV GLKNVTMNEN
     FFVGHFPEAP VMPGVLIVEA MAQTGGILVL STVPDPENYL TYFMKIDNVK FKHKVLPGDT
     LIFKCELISP IRRGICHMQA NAYANGKLVT EAELMAQIVK KQ
//
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