ID A0A1J5FJ25_9BACT Unreviewed; 470 AA.
AC A0A1J5FJ25;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AUK34_06785 {ECO:0000313|EMBL:OIP60180.1};
OS Ignavibacteria bacterium CG2_30_36_16.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805221 {ECO:0000313|EMBL:OIP60180.1, ECO:0000313|Proteomes:UP000183261};
RN [1] {ECO:0000313|EMBL:OIP60180.1, ECO:0000313|Proteomes:UP000183261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_36_16 {ECO:0000313|EMBL:OIP60180.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIP60180.1}.
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DR EMBL; MNYQ01000108; OIP60180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FJ25; -.
DR STRING; 1805221.AUK34_06785; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000183261; 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; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 290
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
FT ACT_SITE 369
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 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00388"
SQ SEQUENCE 470 AA; 52057 MW; A737DA03F4E22DF3 CRC64;
MLETQRTIGK SVSMSGIGLH TGTSCTMTFK PAPDNYGIRF VRVDLGGSPE IPANADNVVD
VSRGTTLAIG EARVHTVEHV LAAVAGLQID NIIIELDGVE PPIGDGSALP YVEVLNKAGF
EQQKAPKDYL IIDETVMFHN DENQVDIVAL PLDDFRVTVM VDYQNPALGS QHTGLFNLDT
EFVSEFAPAR TFCFLSEVEK LSNSGLIKGG DLDNAIVIVD HDLSKQELEA LRKKVGLKRH
FKLGDNGILN NKQLRFRNEP VRHKLLDLLG DLTLIGAPLK AQILAARPGH KSNVEFAKQV
RKLYQQKKIV KKYQLVKKEG IVFDVEAIMR ILPHRYPFLL VDKIIHLEFD KKVIGVKSVT
SNEPFFPGHF PGQPIMPGVL IVEAMAQTGG ILLLNSFPDP AKKLVMFMGI NNVKFRKPVV
PGDQLFLEIE LGARRSKVVN MKGKAYVNEQ LVAEGEFMAA IIDREEIIEE
//
