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G2S4J2 (G2S4J2_ENTAL) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
Gene names
Name:fadB HAMAP-Rule MF_01621
Ordered Locus Names:Entas_4232 EMBL AEN66937.1
OrganismEnterobacter asburiae (strain LF7a) [Complete proteome] [HAMAP] EMBL AEN66937.1
Taxonomic identifier640513 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate By similarity. HAMAP-Rule MF_01621 SAAS SAAS012799

Catalytic activity

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. SAAS SAAS012799 HAMAP-Rule MF_01621

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. SAAS SAAS012799 HAMAP-Rule MF_01621

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. SAAS SAAS012799 HAMAP-Rule MF_01621

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP-Rule MF_01621 SAAS SAAS012799

Pathway

Lipid metabolism; fatty acid beta-oxidation. SAAS SAAS012799 HAMAP-Rule MF_01621

Subunit structure

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity. SAAS SAAS012799 HAMAP-Rule MF_01621

Sequence similarities

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. HAMAP-Rule MF_01621

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. HAMAP-Rule MF_01621

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding400 – 4023NAD By similarity HAMAP-Rule MF_01621
Nucleotide binding427 – 4293NAD By similarity HAMAP-Rule MF_01621
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity HAMAP-Rule MF_01621
Region311 – 7294193-hydroxyacyl-CoA dehydrogenase By similarity HAMAP-Rule MF_01621

Sites

Active site1161For enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities By similarity HAMAP-Rule MF_01621
Active site4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity HAMAP-Rule MF_01621
Binding site2961Substrate By similarity HAMAP-Rule MF_01621
Binding site3241NAD; via amide nitrogen By similarity HAMAP-Rule MF_01621
Binding site3431NAD By similarity HAMAP-Rule MF_01621
Binding site4071NAD By similarity HAMAP-Rule MF_01621
Binding site4531NAD By similarity HAMAP-Rule MF_01621
Binding site5001Substrate By similarity HAMAP-Rule MF_01621
Binding site6601Substrate By similarity HAMAP-Rule MF_01621
Site1191Important for catalytic activity By similarity HAMAP-Rule MF_01621
Site1391Important for catalytic activity By similarity HAMAP-Rule MF_01621

Sequences

Sequence LengthMass (Da)Tools
G2S4J2 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: CF0478D721DCC6B7

FASTA72979,503
        10         20         30         40         50         60 
MLYKGDTLYL NWLEDGIAEL VFDAPGSVNK LDTATVASLG QALDVLEKQS DLKGLLLRSN 

        70         80         90        100        110        120 
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTISAVN GYALGGGCEC 

       130        140        150        160        170        180 
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGAEQAQK 

       190        200        210        220        230        240 
IGLVDGVVKP EKLVEGAIAI LRQAINGDLD WKAKRQPKLE PLKLSKIEAA MSFTIAKGMV 

       250        260        270        280        290        300 
MQTAGKHYPA PITAVKTIEA AARFGREEAL KLENQSFVPL AHTNEARALV GIFLNDQFVK 

       310        320        330        340        350        360 
GKAKQLTKNV ETPKHAAVLG AGIMGGGIAY QSAWKGVPVV MKDISEKSLT LGMTEAAKLL 

       370        380        390        400        410        420 
NKQLERGKID GLKLAGVIST IQPTLEYSGF DRVDVVVEAV VENPKVKKAV LAETEDKVRQ 

       430        440        450        460        470        480 
DTVLASNTST IPISELASVL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS DDTIAKVVAW 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PQRMSKDYRD AIDAMFDANR FGQKNGLGFW RYKEDSKGKP 

       610        620        630        640        650        660 
KKEEDAAVES LLADVSAPKR DFTDEEIIAR MMIPMVNEVV RCLEEGIIAS PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYAVP EGLRNKARHN EPYYPAVEPA 


RPVGELKTA 

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References

[1]"Complete sequence of chromosome of Enterobacter asburiae LF7a."
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., van der Lelie D., Woyke T.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LF7a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003026 Genomic DNA. Translation: AEN66937.1.
RefSeqYP_004830722.1. NC_015968.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEN66937; AEN66937; Entas_4232.
GeneID11110693.
KEGGeas:Entas_4232.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01825.
OMAAKGMVMQ.

Enzyme and pathway databases

BioCycEASB640513:GKDM-4327-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01621. FadB.
InterProIPR006180. 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_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG2S4J2_ENTAL
AccessionPrimary (citable) accession number: G2S4J2
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: April 16, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)