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
	Synonyms:	faoA

From

Pseudomonas fragi

[TaxID: 296]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=B-0771; PubMed=1607366 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A.; "Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation."; J. Biochem. 111:8-15(1992).
[2]	INDUCTION. PubMed=8206878 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Ozeki Y., Kawaguchi A.; "Transcription of the faoAB operon which encodes the HDT multienzyme complex involved in fatty acid beta-oxidation in Pseudomonas fragi B-0771."; J. Biochem. 115:286-292(1994).

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).
INDUCTION: By palmitic acid.
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

D10390; BAA01227.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JX0199; JX0199.

3D structure databases

PDB

1WDK; X-ray; 2.50 A; A/B=1-715.	[ExPASy / RCSB / EBI]
1WDL; X-ray; 3.50 A; A/B=1-715.	[ExPASy / RCSB / EBI]
1WDM; X-ray; 3.80 A; A/B=1-715.	[ExPASy / RCSB / EBI]
2D3T; X-ray; 3.40 A; A/B=1-715.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1WDK; -.
1WDL; -.
1WDM; -.
2D3T; -.

ModBase

P28793.

Protein-protein interaction databases

DIP

DIP:29089N; -.

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; 1.

ProtoNet

P28793.

Other

UniRef

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

Keywords

3D-structure; Direct protein sequencing; 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`	`1 715`	`715`	`Fatty acid oxidation complex subunit alpha.`	`PRO_0000109276`
`REGION`	`1 190`	`190`	`Enoyl-CoA hydratase/isomerase (By similarity).`
`REGION`	`312 715`	`404`	`3-hydroxyacyl-CoA dehydrogenase (By similarity).`
`STRAND`	`6 12`	`7`
`HELIX`	`14 16`	`3`
`STRAND`	`17 22`	`6`
`STRAND`	`27 29`	`3`
`HELIX`	`34 49`	`16`
`STRAND`	`55 67`	`13`
`HELIX`	`71 77`	`7`
`HELIX`	`82 100`	`19`
`STRAND`	`106 110`	`5`
`HELIX`	`117 123`	`7`
`STRAND`	`125 131`	`7`
`STRAND`	`135 137`	`3`
`HELIX`	`139 143`	`5`
`HELIX`	`151 159`	`9`
`HELIX`	`161 170`	`10`
`HELIX`	`176 181`	`6`
`STRAND`	`184 189`	`6`
`HELIX`	`191 193`	`3`
`HELIX`	`194 206`	`13`
`HELIX`	`212 216`	`5`
`HELIX`	`217 220`	`4`
`HELIX`	`227 245`	`19`
`HELIX`	`250 262`	`13`
`HELIX`	`267 282`	`16`
`HELIX`	`285 308`	`24`
`STRAND`	`315 320`	`6`
`HELIX`	`323 335`	`13`
`STRAND`	`340 343`	`4`
`HELIX`	`347 365`	`19`
`TURN`	`366 368`	`3`
`HELIX`	`372 381`	`10`
`STRAND`	`382 388`	`7`
`HELIX`	`391 393`	`3`
`STRAND`	`395 399`	`5`
`HELIX`	`405 416`	`12`
`STRAND`	`424 427`	`4`
`STRAND`	`430 432`	`3`
`HELIX`	`434 437`	`4`
`HELIX`	`438 440`	`3`
`HELIX`	`444 446`	`3`
`STRAND`	`447 451`	`5`
`TURN`	`456 458`	`3`
`STRAND`	`461 466`	`6`
`HELIX`	`472 484`	`13`
`STRAND`	`488 494`	`7`
`TURN`	`496 499`	`4`
`HELIX`	`500 516`	`17`
`HELIX`	`521 531`	`11`
`HELIX`	`537 544`	`8`
`HELIX`	`546 559`	`14`
`HELIX`	`561 564`	`4`
`HELIX`	`571 577`	`7`
`TURN`	`583 586`	`4`
`STRAND`	`587 592`	`6`
`HELIX`	`607 612`	`6`
`HELIX`	`613 615`	`3`
`HELIX`	`624 644`	`21`
`STRAND`	`647 650`	`4`
`HELIX`	`651 661`	`11`
`HELIX`	`666 668`	`3`
`HELIX`	`671 678`	`8`
`HELIX`	`680 689`	`10`
`HELIX`	`690 693`	`4`
`HELIX`	`695 697`	`3`
`HELIX`	`701 708`	`8`

Sequence information

Length: 715 AA [This is the length of the unprocessed precursor]

Molecular weight: 77137 Da [This is the MW of the unprocessed precursor]

CRC64: F22727CDEF7F3DB5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIYEGKAITV TALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIKAD ASVKGVIVSS 

        70         80         90        100        110        120 
GKDVFIVGAD ITEFVENFKL PDAELIAGNL EANKIFSDFE DLNVPTVAAI NGIALGGGLE 

       130        140        150        160        170        180 
MCLAADFRVM ADSAKIGLPE VKLGIYPGFG GTVRLPRLIG VDNAVEWIAS GKENRAEDAL 

       190        200        210        220        230        240 
KVSAVDAVVT ADKLGAAALD LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF 

       250        260        270        280        290        300 
VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LAKTSASNCL IGLFLNDQEL 

       310        320        330        340        350        360 
KKKAKVYDKI AKDVKQAAVL GAGIMGGGIA YQSASKGTPI LMKDINEHGI EQGLAEAAKL 

       370        380        390        400        410        420 
LVGRVDKGRM TPAKMAEVLN GIRPTLSYGD FGNVDLVVEA VVENPKVKQA VLAEVENHVR 

       430        440        450        460        470        480 
EDAILASNTS TISISLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SDLAVATTVA 

       490        500        510        520        530        540 
YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL 

       550        560        570        580        590        600 
MDVVGIDTGH HGRDVMAEGF PDRMKDDRRS AIDALYEAKR LGQKNGKGFY AYEADKKGKQ 

       610        620        630        640        650        660 
KKLVDSSVLE VLKPIVYEQR DVTDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLVY 

       670        680        690        700        710 
GIGFPLFRGG ALRYIDSIGV AEFVALADQY AELGALYHPT AKLREMAKNG QSFFG

P28793 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