Reviewed, UniProtKB/Swiss-Prot A5WH99 (FADB_PSYWF)

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:	PsycPRwf_2100

Organism

Psychrobacter sp. (strain PRwf-1) [Complete proteome] [HAMAP]

Taxonomic identifier

349106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Psychrobacter

Protein attributes

Sequence length	719 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 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 – 719	719	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_1000073634
Regions
	Nucleotide binding	402 – 404	3	NAD By similarity
	Nucleotide binding	429 – 431	3	NAD By similarity
	Region	1 – 190	190	Enoyl-CoA hydratase/isomerase By similarity
	Region	313 – 719	407	3-hydroxyacyl-CoA dehydrogenase By similarity
Sites
	Binding site	298	1	Substrate By similarity
	Binding site	326	1	NAD; via amide nitrogen By similarity
	Binding site	345	1	NAD By similarity
	Binding site	409	1	NAD By similarity
	Binding site	455	1	NAD By similarity
	Binding site	502	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)
	A5WH99-1 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: A736BBCF01D446D7	FASTA	719	78,228
	10 20 30 40 50 60 MIYQGNRITV SLLDDGIANM QFNAEGESVN KFDAETNKQF DEAVSALEKA DNVKGLIVTS 70 80 90 100 110 120 SKGVFIAGAD ITEFVSHFNK EAAEIEKWIV DINGVFNRFE DLPFPKVAAI NGAALGGGCE 130 140 150 160 170 180 MTLVCEYRVM GDKAQIGLPE TQLGIFPGFG GSVRTPRVIG IDNAVELIAT GKAQKPAEAL 190 200 210 220 230 240 KLGLVDAVVA QDDLQEAAVD LVKKCIAGDL DWQAKREEKL QPVKLNQLEQ TMAFSTAKAA 250 260 270 280 290 300 IFAKANPKQY PAPAIAIETI EKHVNLGRDE AIKVEAAGFA KAAKTPQAES LVGLFLNDQT 310 320 330 340 350 360 VKKLAKQHTK NAHDINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ LDLGMGEASK 370 380 390 400 410 420 LLGKMVERKK MTPAQMGETL SRIRPTLNYG DFGETDIVIE AVVENPKVKH AVLKEVEGLV 430 440 450 460 470 480 KDNAILASNT STISITYLAT VLERPENFVG MHFFNPVHRM PLVEVIRGEK SSEEAIATTV 490 500 510 520 530 540 ALAQRMGKVP VVVNDCPGFL VNRVLFPYFG AFDLLLKQGA DFVHVDKVME KFGWPMGPAY 550 560 570 580 590 600 LIDVVGLDTG VHGAEVMAEG FPDRMKPDYK GAIKHLFENN RLGQKNGVGF YKYEKDSRGK 610 620 630 640 650 660 PKKTADDATY ALLKDTTDTD NQQFDDQTII DRMMLAFCNE TVRCLEDNIV ATPSEADMAM 670 680 690 700 710 IMGVGFPAFR GGPCRYIDQV GLDNYLALCE KYAHLGKAYE APQKIRDMAA AGETFYPKA

References

[1]

"Complete sequence of chromosome of Psychrobacter sp. PRwf-1." 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., Kim E., Tiedje J., Richardson P. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000713 Genomic DNA. Translation: ABQ95040.1.
RefSeq	YP_001280990.1.
3D structure databases
SMR	A5WH99. Positions 1-716.
ModBase	Search...
Protein-protein interaction databases
STRING	A5WH99.
Genome annotation databases
GeneID	5206032.
GenomeReviews	Gene locus PsycPRwf_2100 in contig CP000713_GR.
KEGG	prw:PsycPRwf_2100.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HBG691737.
OMA	ASRFGQK.
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. IPR012799. FadB. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00725. 3HCDH. 2 hits. 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_PSYWF

Accession

Primary (citable) accession number: A5WH99

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	July 10, 2007
Last modified:	February 9, 2010
This is version 24 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)