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)
3-hydroxyacyl-CoA dehydrogenase
     (EC 1.1.1.35)

Gene name

	Name:	fadB
	OrderedLocusNames:	Sama_0032

From

Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)

[TaxID: 326297]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; Shewanellaceae; Shewanella.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.;
"Complete sequence of Shewanella amazonensis SB2B.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.

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.
CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O.
CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
PATHWAY: Lipid metabolism; fatty acid beta-oxidation .
SUBUNIT: Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) (By similarity).
SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000507; ABL98244.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_925914.1; -.

3D structure databases

ModBase

A1S1I8.

Ontologies

GO:0016507;	Cellular component: fatty acid beta-oxidation multienzyme complex (inferred from electronic annotation from InterPro).
GO:0003857;	Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0008692;	Molecular function: 3-hydroxybutyryl-CoA epimerase activity (inferred from electronic annotation from HAMAP).
GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004165;	Molecular function: dodecenoyl-CoA delta-isomerase activity (inferred from electronic annotation from HAMAP).
GO:0004300;	Molecular function: enoyl-CoA hydratase activity (inferred from electronic annotation from HAMAP).
GO:0009062;	Biological process: fatty acid catabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01621; -; 1.
PBIL [Tree]

InterPro

IPR006180; 3-OHacyl-CoA_DHase_CS.
IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108; 3HC_DHase_C.
IPR001753; Crotonase_core.
IPR013328; DHase_multihelical.
IPR012799; FadB.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF00725; 3HCDH; 1.
PF02737; 3HCDH_N; 1.
PF00378; ECH; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02437; FadB; 1.

PROSITE

PS00067; 3HCDH; 1.
PS00166; ENOYL_COA_HYDRATASE; FALSE_NEG.

ProtoNet

A1S1I8.

Genome annotation databases

GeneID

4602289; -.

GenomeReviews

CP000507_GR; Sama_0032.

KEGG

saz:Sama_0032; -.

NMPDR

fig|326297.7.peg.28; -.

CMR

A1S1I8; Sama_0032.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Fatty acid metabolism; Isomerase; Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 716`	`716`	`Fatty acid oxidation complex subunit alpha.`	`PRO_1000069572`
`REGION`	`1 188`	`188`	`Enoyl-CoA hydratase/isomerase (By similarity).`
`REGION`	`310 716`	`407`	`3-hydroxyacyl-CoA dehydrogenase (By similarity).`

Sequence information

Length: 716 AA [This is the length of the unprocessed precursor]

Molecular weight: 76369 Da [This is the MW of the unprocessed precursor]

CRC64: 93251CB6B0C3D409 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIYQSPTIQV ELTADKIARL CFNAPGSVNK FDRETLASLN AALDVLKDSD AKAAVLTSGK 

        70         80         90        100        110        120 
DTFIVGADIT EFLALFAEED AKLMEWIAQA NVVFNKLEDL PFPTVSAIKG FALGGGCEAI 

       130        140        150        160        170        180 
LATDFRVADT SAKIGLPETK LGLIPGFGGT VRLPRLIGAD NALEWITTGK DQRPEDALKV 

       190        200        210        220        230        240 
GAIDAVVAPE NLEAAAIQML NDALAGKLDW QARRARKQAP LTLPKLEAMM SFTTAKGMVY 

       250        260        270        280        290        300 
AVAGKHYPAP MAAVSVVEQA AGMSRAEALV VEHNAFIKLA KTDVATALIG IFLNDQLVKG 

       310        320        330        340        350        360 
KAKKASKLAK DIKHAAVLGA GIMGGGIAYQ SASKGTPIVM KDINQAALDL GVNEAAKLLS 

       370        380        390        400        410        420 
AQVARGRSTP DKMAKVLNNI TPALDYAPLK DVNVVVEAVV ENPKVKAMVL ADVENVVADD 

       430        440        450        460        470        480 
AIIASNTSTI SIDLLAKSLK NPARFCGMHF FNPVHKMPLV EVIRGKDTSE ETVASVVAYA 

       490        500        510        520        530        540 
SKMGKTPIVV NDCPGFFVNR VLFPYFAGFN GLLADGGDFA AIDKVMEKQF GWPMGPAYLL 

       550        560        570        580        590        600 
DVVGLDTGHH AQAVMADGFP DRMGKSDKDA IDVMYEAGRL GQKNGKGFYQ YSIDKRGKPK 

       610        620        630        640        650        660 
KDVDPASYTM LAEAFGAQKA FEADEIIART MIPMIIETVR CLEEGIVASP AEADMGLVYG 

       670        680        690        700        710 
LGFPPFRGGV FRYLDTMGVA NFVALADKYA HLGGLYQVTD AMRELASNNG SYYPKA

A1S1I8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools