Reviewed, UniProtKB/Swiss-Prot Q6FF68 (FADB_ACIAD)

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:	ACIAD0335

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	717 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 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 – 717	717	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_0000109264
Regions
	Region	1 – 190	190	Enoyl-CoA hydratase/isomerase By similarity
	Region	313 – 717	405	3-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FF68-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: C0981AB69CA14483	FASTA	717	77,985
	10 20 30 40 50 60 MIHAGNAITV QMLSDGIAEF RFDLQGESVN KFNRATIEDF QAAIEAVKNH PEVKGLIVTS 70 80 90 100 110 120 AKSTFIVGAD ITEFGQNFAQ GEKAIVEWAL PVHDIFNSFE DLDIPKVAAI NGMALGGGFE 130 140 150 160 170 180 MCLVCDYRVM SDQAQVGLPE IKLGIFPGFG GTVRLSRLIG IDNAVEWIAM AAPKKPAAAL 190 200 210 220 230 240 KDGAVDAVVS ADKLQEAAID LVKQALAGRV DWKAKRQEKL NPVKLNPLEQ MMAFNTAKGA 250 260 270 280 290 300 VLAKANPAQY PAPKLMLDSL QAGASLGRDE ALKVETEGFA KAAITPQAEA LIGLFLNDQI 310 320 330 340 350 360 IKKTSKKHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ LALGMQEANG 370 380 390 400 410 420 LLTKQVERKK LTPAKMGETL ARIRPTLSYD EFKEVDIVIE AVTENPKIKE AVLADTEAKV 430 440 450 460 470 480 RDNTIIASNT STISITRLAK ALKRPENFVG MHFFNPVHMM PLVEVIRGEQ TSEEAVATTV 490 500 510 520 530 540 VLAQKMGKTP IVVNDCPGFL VNRVLFPYFG AFDLLLKDGA DFQQIDKVME KFGWPMGPAY 550 560 570 580 590 600 LMDVVGIDTG VHGAEVMAEG FPDRMKPDYK GSIQTMYEAK RLGQKNDVGF YKYELDKKGK 610 620 630 640 650 660 KAKTVDSTAY EVIAPVVTSE KREFDAQEII DRMMLALCNE TVRCLEDNIV ATPAEADMAM 670 680 690 700 710 IMGIGFPPFR GGPCRYIDQT GVAEYVALCN KYAHLGKAYE APQLLRDMAE NNKKFYG

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR543861 Genomic DNA. Translation: CAG67289.1.
RefSeq	YP_045111.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2881154.
GenomeReviews	Gene locus ACIAD0335 in contig CR543861_GR.
KEGG	aci:ACIAD0335.
NMPDR	fig|62977.3.peg.812.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6FF68.
OMA	Q6FF68. ANNGSYY.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0335-MON.
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. IPR013328. DH_multihelical. 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. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADB_ACIAD

Accession

Primary (citable) accession number: Q6FF68

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 39 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)