FABZ_ECOLI
ID FABZ_ECOLI Reviewed; 151 AA.
AC P0A6Q6; P21774;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ;
DE EC=4.2.1.59 {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376};
DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase;
DE Short=(3R)-hydroxymyristoyl-ACP dehydrase;
DE AltName: Full=17 kDa actomyosin component;
DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase;
GN Name=fabZ; Synonyms=sefA, yaeA; OrderedLocusNames=b0180, JW0175;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3277952; DOI=10.1128/jb.170.3.1268-1274.1988;
RA Coleman J., Raetz C.R.H.;
RT "First committed step of lipid A biosynthesis in Escherichia coli: sequence
RT of the lpxA gene.";
RL J. Bacteriol. 170:1268-1274(1988).
RN [2]
RP SEQUENCE REVISION TO 140-141 AND 150-151.
RA Coleman J.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 2-18, SIMILARITY, AND POSSIBLE FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8354462; DOI=10.1111/j.1574-6968.1993.tb06338.x;
RA Foster S.J.;
RT "Purification and characterization of an 'actomyosin' complex from
RT Escherichia coli W3110.";
RL FEMS Microbiol. Lett. 110:295-298(1993).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7806516; DOI=10.1016/s0021-9258(20)30075-2;
RA Mohan S., Kelly T.M., Eveland S.S., Raetz C.R.H., Anderson M.S.;
RT "An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl
RT carrier protein dehydrase. Relation to fabA and suppression of mutations in
RT lipid A biosynthesis.";
RL J. Biol. Chem. 269:32896-32903(1994).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=8910376; DOI=10.1074/jbc.271.44.27795;
RA Heath R.J., Rock C.O.;
RT "Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein
RT dehydratases in Escherichia coli fatty acid biosynthesis.";
RL J. Biol. Chem. 271:27795-27801(1996).
RN [10]
RP MUTAGENESIS OF LEU-85.
RC STRAIN=K12 / W3110, and W2252;
RX PubMed=10048027; DOI=10.1046/j.1365-2958.1999.01221.x;
RA Ogura T., Inoue K., Tatsuta T., Suzaki T., Karata K., Young K., Su L.H.,
RA Fierke C.A., Jackman J.E., Raetz C.R., Coleman J., Tomoyasu T.,
RA Matsuzawa H.;
RT "Balanced biosynthesis of major membrane components through regulated
RT degradation of the committed enzyme of lipid A biosynthesis by the AAA
RT protease FtsH (HflB) in Escherichia coli.";
RL Mol. Microbiol. 31:833-844(1999).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10629181; DOI=10.1128/jb.182.2.365-370.2000;
RA Choi K.-H., Heath R.J., Rock C.O.;
RT "Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining
RT factor in branched-chain fatty acid biosynthesis.";
RL J. Bacteriol. 182:365-370(2000).
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:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516,
CC ECO:0000269|PubMed:8910376}.
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:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516,
CC ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098;
CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516,
CC ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453;
CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462;
CC Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472;
CC Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475;
CC Evidence={ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC Evidence={ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481;
CC Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxy-(9Z)-hexadecenoyl-[ACP] = (2E,9Z)-
CC hexadecadienoyl-[ACP] + H2O; Xref=Rhea:RHEA:54932, Rhea:RHEA-
CC COMP:14036, Rhea:RHEA-COMP:14040, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:138403, ChEBI:CHEBI:138407;
CC Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54933;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxy-5-methylhexanoyl-[ACP] = (2E)-5-methylhexenoyl-
CC [ACP] + H2O; Xref=Rhea:RHEA:55128, Rhea:RHEA-COMP:14095, Rhea:RHEA-
CC COMP:14097, ChEBI:CHEBI:15377, ChEBI:CHEBI:78986, ChEBI:CHEBI:138610;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55129;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- SUBUNIT: Oligomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC subfamily. {ECO:0000305}.
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DR EMBL; M19334; AAC36917.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73291.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77855.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08609.1; -; Genomic_DNA.
DR PIR; D64742; D64742.
DR RefSeq; NP_414722.1; NC_000913.3.
DR RefSeq; WP_000210739.1; NZ_STEB01000032.1.
DR PDB; 6N3P; X-ray; 2.50 A; A/B/C/D/E/F=1-150.
DR PDBsum; 6N3P; -.
DR AlphaFoldDB; P0A6Q6; -.
DR SMR; P0A6Q6; -.
DR BioGRID; 4263243; 437.
DR DIP; DIP-31868N; -.
DR IntAct; P0A6Q6; 34.
DR STRING; 511145.b0180; -.
DR SwissLipids; SLP:000001787; -.
DR jPOST; P0A6Q6; -.
DR PaxDb; P0A6Q6; -.
DR PRIDE; P0A6Q6; -.
DR EnsemblBacteria; AAC73291; AAC73291; b0180.
DR EnsemblBacteria; BAA77855; BAA77855; BAA77855.
DR GeneID; 67416256; -.
DR GeneID; 944888; -.
DR KEGG; ecj:JW0175; -.
DR KEGG; eco:b0180; -.
DR PATRIC; fig|1411691.4.peg.2099; -.
DR EchoBASE; EB1261; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_078912_1_0_6; -.
DR InParanoid; P0A6Q6; -.
DR OMA; FPGRPLM; -.
DR PhylomeDB; P0A6Q6; -.
DR BioCyc; EcoCyc:FABZ-MON; -.
DR BioCyc; MetaCyc:FABZ-MON; -.
DR PRO; PR:P0A6Q6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IDA:EcoCyc.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IDA:EcoCyc.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00406; FabZ; 1.
DR InterPro; IPR013114; FabA_FabZ.
DR InterPro; IPR010084; FabZ.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR30272; PTHR30272; 1.
DR Pfam; PF07977; FabA; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR01750; fabZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Reference proteome.
FT CHAIN 1..151
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000091673"
FT ACT_SITE 54
FT /evidence="ECO:0000250"
FT MUTAGEN 85
FT /note="L->P: In sfhC21; suppresses an ftsH deletion mutant
FT as well as an ftsH temperature-sensitive mutation. Probably
FT stabilizes the enzyme."
FT /evidence="ECO:0000269|PubMed:10048027"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:6N3P"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:6N3P"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6N3P"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6N3P"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6N3P"
FT HELIX 63..81
FT /evidence="ECO:0007829|PDB:6N3P"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:6N3P"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:6N3P"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:6N3P"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:6N3P"
SQ SEQUENCE 151 AA; 17033 MW; 91F514A7319C2FB1 CRC64;
MTTNTHTLQI EEILELLPHR FPFLLVDRVL DFEEGRFLRA VKNVSVNEPF FQGHFPGKPI
FPGVLILEAM AQATGILAFK SVGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVTFEKT
RRGLTRFKGV ALVDGKVVCE ATMMCARSRE A
