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:	Sfri_0013

From

Shewanella frigidimarina (strain NCIMB 400)

[TaxID: 318167]

[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., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
"Complete sequence of Shewanella frigidimarina NCIMB 400.";
Submitted (AUG-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

CP000447; ABI69876.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_748714.1; -.

3D structure databases

ModBase

Q08A39.

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

Q08A39.

Genome annotation databases

GeneID

4277696; -.

GenomeReviews

CP000447_GR; Sfri_0013.

KEGG

sfr:Sfri_0013; -.

NMPDR

fig|318167.10.peg.13; -.

Phylogenomic databases

HOGENOM

Q08A39; -.

Genome annotation databases

CMR

Q08A39; Sfri_0013.

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_1000069575`
`REGION`	`1 189`	`189`	`Enoyl-CoA hydratase/isomerase (By similarity).`
`REGION`	`311 716`	`406`	`3-hydroxyacyl-CoA dehydrogenase (By similarity).`

Sequence information

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

Molecular weight: 76897 Da [This is the MW of the unprocessed precursor]

CRC64: 28434AB7ABC1166C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIYQSPTIQV ELLEDNIAKL CFNAQGSVNK FDRETIASLD AALDSIKQNT NIKALLLTSA 

        70         80         90        100        110        120 
KSTFIVGADI TEFLTLFQQD DATLLAWVEQ ANAVFNKLED LPFPTASAIN GFALGGGCET 

       130        140        150        160        170        180 
ILATDLRVAD TNARIGLPET KLGLIPGFGG TVRLPRVIGA DNALEWITTA KDQRPEDALK 

       190        200        210        220        230        240 
VGAIDAVVAP ENLEAAAIQM LHDALNGSLD WQARRTKKQS PLQLPKLEAM MSFATAKGMV 

       250        260        270        280        290        300 
FSVAGKHYPA PMAAVNVVEQ AAGLDRDGAL KVEALAFIKL AKTDVAQALI GIFLNDQFVK 

       310        320        330        340        350        360 
GKAKKAGKLA KDVNQAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALE LGLNEAAKIL 

       370        380        390        400        410        420 
TTQVARGRST PEKMAKVLNN ITPSLDYAAI KNSDIVVEAV VEHPKVKATV LAEVEGYVSE 

       430        440        450        460        470        480 
DAIIASNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEIIRGEHSS EETIATVVAY 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLAEGADF AAVDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGLDTGH HAQAVMAEGF PDRMGKNGKD AIDIMFENKR LGQKNTKGFY AYSVDRRGKP 

       610        620        630        640        650        660 
KKDIDPTSYE LLSAEFGELK AFESDDIIAR CMIPMIIETV RCLEEGIIAS PAEGDMGLVY 

       670        680        690        700        710 
GIGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT DAMRALAANN GSYYQA

Q08A39 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