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Reviewed, UniProtKB/Swiss-Prot Q57HM6 (FADB_SALCH)

Last modified February 9, 2010. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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: SCH_3880
OrganismSalmonella choleraesuis [Complete proteome] [HAMAP]
Taxonomic identifier28901 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Fatty acid oxidation complex subunit alpha HAMAP MF_01621
PRO_0000109284

Regions

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

Sites

Binding site2961Substrate By similarity
Binding site3241NAD; via amide nitrogen By similarity
Binding site3431NAD By similarity
Binding site4071NAD By similarity
Binding site4531NAD By similarity
Binding site5001Substrate By similarity
Binding site6601Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q57HM6-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 91F7AF5A267F429D

FASTA72979,608
        10         20         30         40         50         60 
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG QALEVLEKQH DLKGLLLRSN 

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

       130        140        150        160        170        180 
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRLPRMLGA DSALEIIAAG KDVGAEHALK 

       190        200        210        220        230        240 
IGLVDGVVKQ EKLIEGAIAV LRQAITGDLD WRAKRQPKLE PLKLSKIEAA MSFTIAKGMV 

       250        260        270        280        290        300 
AQTAGKHYPA PMTAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
GKAKKLTKDI ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLN LGMTEAAKLL 

       370        380        390        400        410        420 
NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRP 

       430        440        450        460        470        480 
ETVLASNTST IPIGELASAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW 

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

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PQRMQKEYRD AIDALFDASR FGQKNGLGFW RYKEDSKGKP 

       610        620        630        640        650        660 
KKEEDAAVDD LLASVSQPKR DFSDDEIIAR MMIPMINEVV RCLEEGIIAS PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG AFRWLDTQGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA 


RPVGSLKTA

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References

[1]"The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen."
Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.
Nucleic Acids Res. 33:1690-1698(2005) [PubMed: 15781495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC-B67.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017220 Genomic DNA. Translation: AAX67786.1. Different initiation.
RefSeqYP_218867.2.

3D structure databases

SMRQ57HM6. Positions 1-714.
ModBaseSearch...

Genome annotation databases

GeneID3336414.
GenomeReviewsGene locus SCH_3880 in contig AE017220_GR.
KEGGsec:SC3880.
NMPDRfig|321314.4.peg.3209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG691737.
OMAASRFGQK.

Enzyme and pathway databases

BioCycSENT321314:SCH_3880-MONOMER.
BRENDA1.1.1.35. 276841.
4.2.1.17. 276841.
5.1.2.3. 276841.
5.3.3.8. 276841.

Family and domain databases

HAMAPMF_01621. FadB.
[Tree]
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.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFADB_SALCH
AccessionPrimary (citable) accession number: Q57HM6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: February 9, 2010
This is version 38 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents