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Q9KNI1 (FADB_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

  1. Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
    EC=4.2.1.17
    EC=5.1.2.3
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:fadB
Ordered Locus Names:VC_2758
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity. HAMAP-Rule MF_01621

Catalytic activity

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

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

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

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

Pathway

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

Subunit structure

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 723723Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000255846

Regions

Nucleotide binding401 – 4033NAD By similarity
Nucleotide binding428 – 4303NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7234133-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Binding site2961Substrate By similarity
Binding site3251NAD; via amide nitrogen By similarity
Binding site3441NAD By similarity
Binding site4081NAD By similarity
Binding site4541NAD By similarity
Binding site5011Substrate By similarity
Binding site6611Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KNI1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 147F5ABD0B0797F8

FASTA72378,108
        10         20         30         40         50         60 
MIYQAKTLQV KQLANGIAEL SFCAPASVNK LDLHTLESLD KALDALAADS SVKGLLLSSD 

        70         80         90        100        110        120 
KEAFIVGADI TEFLGLFAKP EAELDEWLQF ANRIFNKLED LPFPTLSALK GHTLGGGCEC 

       130        140        150        160        170        180 
VLATDFRIGD ATTSIGLPET KLGIMPGFGG TVRLPRLIGA DSAMEIITQG KACRAEEALK 

       190        200        210        220        230        240 
VGLLDAIVDS DKLIDSAITT LTQAIEEKLD WQKRRQQKTS ALTLSKLEAM MSFTMAKGMV 

       250        260        270        280        290        300 
AQVAGKHYPA PMTSVVTIEE AARLPRDAAL DIERKHFIKL AKSTEAQALV GIFLNDQYIK 

       310        320        330        340        350        360 
GLAKQSAKAA SQDTQHAAVL GAGIMGGGIA YQSALKGVPV LMKDIAPHSL ELGMTEAAKL 

       370        380        390        400        410        420 
LNKQLERGKI DGFKMAGILA SITPSLHYAG IDQADVIVEA VVENPKVKAA VLSEVEGLVD 

       430        440        450        460        470        480 
TETILTSNTS TIPINLLAKS LKRPQNFCGM HFFNPVHRMP LVEIIRGEHT SEDTINRVVA 

       490        500        510        520        530        540 
YAAKMGKSPI VVNDCPGFFV NRVLFPYFAG FSLLMRDGAN FTEIDKVMER QFGWPMGPAY 

       550        560        570        580        590        600 
LLDVVGIDTA HHAQAVMAEG FPTRMAKSGR EAIDALYEAK KFGQKNGSGF YQYTVDKKGK 

       610        620        630        640        650        660 
PKKAFSDDVL AILAPVCGAP QSFDPQTLIE RTMIPMINEV VLCLEEGIIA SAQEADMALV 

       670        680        690        700        710        720 
YGLGFPPFRG GVFRYLDTIG IANYVAMAEK YADLGALYQV PQLLKNMAQQ GTSFYSAQQV 


SAL

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003852 Genomic DNA. Translation: AAF95897.1.
PIRH82035.
RefSeqNP_232384.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KNI1.
SMRQ9KNI1. Positions 1-716.
ModBaseSearch...

Protein-protein interaction databases

STRING243277.VC2758.

Protocols and materials databases

DNASU2614935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF95897; AAF95897; VC_2758.
GeneID2614935.
KEGGvch:VC2758.
PATRIC20084562. VBIVibCho83274_2633.

Phylogenomic databases

eggNOGCOG1250.
KOK01825.
OMAGLYPGFG.
ProtClustDBPRK11730.

Enzyme and pathway databases

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.
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. 6DGDH_C_like. 2 hits.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_VIBCH
AccessionPrimary (citable) accession number: Q9KNI1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2000
Last modified: May 29, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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