Reviewed, UniProtKB/Swiss-Prot A5W6H0 (FADB_PSEP1)

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:	Pput_3606

Organism

Pseudomonas putida (strain F1 / ATCC 700007) [Complete proteome] [HAMAP]

Taxonomic identifier

351746 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	715 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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 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 – 715	715	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_1000069569
Regions
	Region	1 – 190	190	Enoyl-CoA hydratase/isomerase By similarity
	Region	312 – 715	404	3-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5W6H0-1 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: 7E078AD847B4FB3C	FASTA	715	77,397
	10 20 30 40 50 60 MIYEGKAITV KALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIRAD ASVKGVIVSS 70 80 90 100 110 120 GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFNAFE DLEVPTVAAI NGIALGGGLE 130 140 150 160 170 180 MCLAADYRVM STSARIGLPE VKLGIYPGFG GTVRLPRLIG SDNAIEWIAA GKENRAEDAL 190 200 210 220 230 240 KVGAVDAVVA PELLLAGALD LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF 250 260 270 280 290 300 VAGQAGPNYP APVEAIKSIQ KAANFGRDKA LEVEAAGFAK LAKTSVAESL IGLFLNDQEL 310 320 330 340 350 360 KRKAKAHDEI AHDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI QLGLNEASKL 370 380 390 400 410 420 LGNRVEKGRL TPAKMAEALN AIRPTLSYGD FANVDIVVEA VVENPKVKQA VLAEVEGQVK 430 440 450 460 470 480 DDAILASNTS TISINLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SDVAVATTVA 490 500 510 520 530 540 YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL 550 560 570 580 590 600 MDVVGIDTGH HGRDVMAEGF PDRMKDERRS AVDALYESNR LGQKNGKGFY AYETDKRGKP 610 620 630 640 650 660 KKVFDATVLD VLKPIVFEQR EVTDEDIINW MMVPLCLETV RCLEDGIVET AAEADMGLVY 670 680 690 700 710 GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGPLYHPT AKLREMAKNG QRFFN

References

[1]

"Complete sequence of Pseudomonas putida F1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000712 Genomic DNA. Translation: ABQ79730.1.
RefSeq	YP_001268914.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5190372.
GenomeReviews	Gene locus Pput_3606 in contig CP000712_GR.
KEGG	ppf:Pput_3606.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A5W6H0. QFANSIF.
Family and domain databases
HAMAP	MF_01621. [Tree]
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR001753. Crotonase_core. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012799. FadB. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADB_PSEP1

Accession

Primary (citable) accession number: A5W6H0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 10, 2007
Last modified:	June 16, 2009
This is version 17 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)