FABZ_PSEAE
ID FABZ_PSEAE Reviewed; 146 AA.
AC Q9HXY7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000255|HAMAP-Rule:MF_00406};
DE EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00406};
DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00406};
DE Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000255|HAMAP-Rule:MF_00406};
DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000255|HAMAP-Rule:MF_00406};
GN Name=fabZ {ECO:0000255|HAMAP-Rule:MF_00406}; OrderedLocusNames=PA3645;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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. {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_00406};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00406}.
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DR EMBL; AE004091; AAG07033.1; -; Genomic_DNA.
DR PIR; E83190; E83190.
DR RefSeq; NP_252335.1; NC_002516.2.
DR RefSeq; WP_003092375.1; NZ_QZGE01000001.1.
DR PDB; 1U1Z; X-ray; 2.50 A; A/B/C/D/E/F=1-146.
DR PDBsum; 1U1Z; -.
DR AlphaFoldDB; Q9HXY7; -.
DR SMR; Q9HXY7; -.
DR STRING; 287.DR97_4294; -.
DR PaxDb; Q9HXY7; -.
DR PRIDE; Q9HXY7; -.
DR DNASU; 880494; -.
DR EnsemblBacteria; AAG07033; AAG07033; PA3645.
DR GeneID; 880494; -.
DR KEGG; pae:PA3645; -.
DR PATRIC; fig|208964.12.peg.3814; -.
DR PseudoCAP; PA3645; -.
DR HOGENOM; CLU_078912_1_0_6; -.
DR InParanoid; Q9HXY7; -.
DR OMA; FPGRPLM; -.
DR PhylomeDB; Q9HXY7; -.
DR BioCyc; PAER208964:G1FZ6-3715-MON; -.
DR EvolutionaryTrace; Q9HXY7; -.
DR Proteomes; UP000002438; 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; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase 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 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; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Reference proteome.
FT CHAIN 1..146
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000091713"
FT ACT_SITE 49
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1U1Z"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1U1Z"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1U1Z"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:1U1Z"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1U1Z"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1U1Z"
FT HELIX 58..77
FT /evidence="ECO:0007829|PDB:1U1Z"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:1U1Z"
FT STRAND 106..117
FT /evidence="ECO:0007829|PDB:1U1Z"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:1U1Z"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:1U1Z"
SQ SEQUENCE 146 AA; 16774 MW; BC7D53E61F5E44CB CRC64;
MMDINEIREY LPHRYPFLLV DRVVELDIEG KRIRAYKNVS INEPFFNGHF PEHPIMPGVL
IIEAMAQAAG ILGFKMLDVK PADGTLYYFV GSDKLRFRQP VLPGDQLQLH AKFISVKRSI
WKFDCHATVD DKPVCSAEII CAERKL
