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Database: UniProt
Entry: A0A0M8M7S8_9FLAO
LinkDB: A0A0M8M7S8_9FLAO
Original site: A0A0M8M7S8_9FLAO 
ID   A0A0M8M7S8_9FLAO        Unreviewed;       463 AA.
AC   A0A0M8M7S8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=AM493_03445 {ECO:0000313|EMBL:KOS05193.1};
OS   Flavobacterium akiainvivens.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS05193.1, ECO:0000313|Proteomes:UP000037755};
RN   [1] {ECO:0000313|EMBL:KOS05193.1, ECO:0000313|Proteomes:UP000037755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IK-1 {ECO:0000313|EMBL:KOS05193.1,
RC   ECO:0000313|Proteomes:UP000037755};
RA   Wan X., Hou S., Saito J., Donachie S.;
RT   "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT   Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL   Submitted (AUG-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:KOS05193.1}.
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DR   EMBL; LIYD01000005; KOS05193.1; -; Genomic_DNA.
DR   RefSeq; WP_054406261.1; NZ_LIYD01000005.1.
DR   AlphaFoldDB; A0A0M8M7S8; -.
DR   STRING; 1202724.AM493_03445; -.
DR   PATRIC; fig|1202724.3.peg.707; -.
DR   OrthoDB; 9772788at2; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000037755; 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:UP000037755};
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   463 AA;  51006 MW;  826B39AD425C4007 CRC64;
     MVKQTTIRSE VSLKGVGLHT GKEVTMTFKP APVNNGYTFV RVDLEGKPVI EADATYVVNT
     QRGTNLEKNG VKIQTSEHVL AAFVGCDVDN VIIELNASEP PIMDGSSKFF VEAIESVGVE
     EQDAERKVYV VKEVISYTDE ATGSEIIVMP ADEYQVTTMV DFGTKVLGTQ NATLKSMGDF
     KEEIADARTF SFLHELETLL EHGLIKGGDL NNAIVYVDKE ISPETMDRLK VAFGKESISV
     KPNGILDNLT LHYPNEAARH KLLDVVGDLA LIGTRIKGKV IANKPGHFVN TQFAKKIAKL
     IKIEQRNAVP VYDLHKEPLM DIHKIMAMLP HRPPFLLVDR ILEMSDNHVV GLKNVTMNES
     FFVGHFPGAP VMPGVLIVEA MAQTGGILIL STVPDPENYL TYFMKIDGVK FKHKVLPGDT
     LVFKCDLVSP IRRGICHMHA NAYANGKLVA EAELMAQIAK NNN
//
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