Reviewed, UniProtKB/Swiss-Prot Q4ZRA0 (FADB_PSEU2)

Names and origin

Protein names

Recommended name:
    Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
              EC=4.2.1.17
              EC=5.3.3.8
              EC=5.1.2.3
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35

Gene names

Name:	fadB
Ordered Locus Names:	Psyr_3290

Organism

Pseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP]

Taxonomic identifier

205918 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas syringae

Protein attributes

Sequence length	721 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity. HAMAP MF_01621
Catalytic activity	(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01621 (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01621 (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01621 (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP MF_01621
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01621
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. HAMAP MF_01621
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	fatty acid beta-oxidation multienzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 3-hydroxybutyryl-CoA epimerase activity Inferred from electronic annotation. Source: HAMAP coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: HAMAP enoyl-CoA hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 721	721	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_0000109281
Regions
	Nucleotide binding	401 – 403	3	NAD By similarity
	Nucleotide binding	428 – 430	3	NAD By similarity
	Region	1 – 190	190	Enoyl-CoA hydratase/isomerase By similarity
	Region	312 – 721	410	3-hydroxyacyl-CoA dehydrogenase By similarity
Sites
	Binding site	297	1	Substrate By similarity
	Binding site	325	1	NAD; via amide nitrogen By similarity
	Binding site	344	1	NAD By similarity
	Binding site	408	1	NAD By similarity
	Binding site	454	1	NAD By similarity
	Binding site	501	1	Substrate By similarity
	Binding site	660	1	Substrate By similarity
	Site	120	1	Important for catalytic activity By similarity
	Site	140	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4ZRA0-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 5C9890C2DCCF54EB	FASTA	721	77,709
	10 20 30 40 50 60 MIYEGKAITV KALESGIVEL NFDLKGESVN KFNRLTLNEF RQAVDAVKAD ASVKGVIVTS 70 80 90 100 110 120 GKDSFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFSDFE DLNVPTVVAI NGIALGGGLE 130 140 150 160 170 180 MCLAADYRVM ASSARIGLPE VKLGLYPGFG GTVRLPRIIG ADNAIEWIAS GKENAAEDAL 190 200 210 220 230 240 KVGAVDAVVA PEKLQAAALD LIQRAISGEF DYKAKRQPKL DKLKLNAIEQ MMAFETAKGF 250 260 270 280 290 300 VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEIEAAGFVK MAKTPAAQSL IGLFLNDQEL 310 320 330 340 350 360 KKKARGYDKI AKDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI QLGLNEASKL 370 380 390 400 410 420 LGGRLEKGRL TAAKMAEALN AIRPTLSYGD FGNVDLVVEA VVENPKVKQA VLAEVEANVG 430 440 450 460 470 480 ENTILASNTS TISISLLAQA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SEEAVATTVA 490 500 510 520 530 540 YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FARLVSAGVD FVRIDKVMEK FGWPMGPAYL 550 560 570 580 590 600 MDVVGIDTGH HGRDVMAEGF PDRMKDDRRS AIDALYDAKR LGQKNGKGFY AYETDKKGKP 610 620 630 640 650 660 KKVNDPAVLD VLKPIVYEQR EVSDEDIVNW MMIPLCLETV RCLEDGIVET AAEADMGLIY 670 680 690 700 710 720 GIGFPPFRGG ALRYIDSIGV AEFVALADQY AELGALYQPT AKLREMAANG QSFFGQASSE E

References

[1]

"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000." Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E. Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed: 16043691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000075 Genomic DNA. Translation: AAY38322.1.
RefSeq	YP_236360.1.
3D structure databases
SMR	Q4ZRA0. Positions 1-715.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4ZRA0.
Genome annotation databases
GeneID	3368817.
GenomeReviews	Gene locus Psyr_3290 in contig CP000075_GR.
KEGG	psb:Psyr_3290.
NMPDR	fig|205918.4.peg.3585.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HBG691737.
OMA	YFGGFAR.
Enzyme and pathway databases
BioCyc	PSYR205918:PSYR_3290-MONOMER.
Family and domain databases
HAMAP	MF_01621. FadB. [Tree]
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR001753. Crotonase_core. IPR013328. DH_multihelical. IPR012799. FadB. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
Pfam	PF00725. 3HCDH. 1 hit. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
TIGRFAMs	TIGR02437. FadB. 1 hit.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADB_PSEU2

Accession

Primary (citable) accession number: Q4ZRA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	June 7, 2005
Last modified:	February 9, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)