1U1Z

The Structure of (3R)-hydroxyacyl-ACP dehydratase (FabZ)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1u1za_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
B	d1u1zb_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
C	d1u1zc1	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
C	d1u1zc2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
D	d1u1zd_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
E	d1u1ze_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
F	d1u1zf_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	FabZ-like	8028281	4002539	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040660	3000149	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040660	3000149	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040660	3000149	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040660	3000149	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040660	3000149	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8040660	3000149	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	FabA	e1u1zA1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
B	FabA	e1u1zB1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
C	FabA	e1u1zC1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
D	FabA	e1u1zD1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
E	FabA	e1u1zE1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
F	FabA	e1u1zF1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
B	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
C	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
D	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
E	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
F	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF07977	FabA-like domain (FabA)	FabA-like domain	This enzyme domain has a HotDog fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	(3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase	(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process cellular lipid metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process cellular lipid metabolic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process glycolipid metabolic process lipid A biosynthetic process carbohydrate derivative metabolic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process liposaccharide metabolic process glycolipid biosynthetic process phospholipid biosynthetic process lipid A metabolic process organophosphate metabolic process organophosphate biosynthetic process membrane lipid biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR010084	Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ	Family
A, B, C, D, E A, B, C, D, E, F	IPR013114	Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ	Family
A, B, C, D, E A, B, C, D, E, F	IPR029069	HotDog domain superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A, B	3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ M-CSA #947	FabZ is the primary dehydratase involved in fatty-acid elongation in type II fatty acid biosynthesis (FAS). Involved in unsaturated fatty acids biosynthesis. Catalyses the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.	Defined by 5 residues: HIS:A-69 [auth A-49]ILE:A-75 [auth A-55]GLY:A-78 [auth A-58]VAL:A-79 [auth A-59]GLU:B-83 [auth B-63] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.2.1 (PDB Primary Data) Search M-CSA Motif + EC 4.2.1 EC: 4.2.1.59 (UniProt) Search M-CSA Motif + EC 4.2.1.59

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.