Fatty acid oxidation complex subunit alpha - Photorhabdus luminescens subsp. laumondii

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Reviewed, UniProtKB/Swiss-Prot Q7MZ92 (FADB_PHOLL)

Last modified February 9, 2010. Version 47. History...

Clusters with 100%, 90%, 50% identity |

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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 names

Recommended 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:	plu4402

Organism

Photorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]

Taxonomic identifier

141679 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus

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Protein attributes

Sequence length	728 AA.
Sequence status	Complete.
Protein existence	Inferred 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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Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	fatty acid beta-oxidation multienzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 3-hydroxybutyryl-CoA epimerase activity Inferred from electronic annotation. Source: HAMAP coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: HAMAP enoyl-CoA hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 728

728

Fatty acid oxidation complex subunit alpha HAMAP MF_01621

PRO_0000109273

Regions

Nucleotide binding

400 – 402

NAD By similarity

Nucleotide binding

427 – 429

NAD By similarity

Region

1 – 189

189

Enoyl-CoA hydratase/isomerase By similarity

Region

311 – 728

418

3-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Binding site

296

Substrate By similarity

Binding site

324

NAD; via amide nitrogen By similarity

Binding site

343

NAD By similarity

Binding site

407

NAD By similarity

Binding site

453

NAD By similarity

Binding site

500

Substrate By similarity

Binding site

660

Substrate By similarity

Site

119

Important for catalytic activity By similarity

Site

139

Important for catalytic activity By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q7MZ92-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 4168E8DF36B2E4C2
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FASTA

728

79,352

        10         20         30         40         50         60 
MLYQSETIQV SWLKDGIAEL VFNAPAAINK LDTKTVASLD KAIASLEQQT GLKGVLLRSE 

        70         80         90        100        110        120 
KTAFIVGADI TEFLSLFDSP VEKLQEWLNF SNSIFNRIED LPVPTISAIN GYALGGGCEC 

       130        140        150        160        170        180 
VLSTDFRVAS PDIRIGLPET KLGIMPGFGG SVRLPRLIGT DNALDIIAAG KDIGAEEALK 

       190        200        210        220        230        240 
NGLIDAVVPK EKLVDSAVSM LEQAIAGNLD WKAARQPKLE PLKLNETERG MSFSVAKGMV 

       250        260        270        280        290        300 
MKVAGPHYPA PITAVKSIEK AATFGRDEAL KQETASFIPL AQTNVARALV GIFLNDQYVK 

       310        320        330        340        350        360 
GLAKKHLKEV TIPEYAAVLG AGIMGGGIAY QSARKGIPVM MKDISQQSLE LGMNEAAKLL 

       370        380        390        400        410        420 
NKQFERGRLD AIKMARTLSS IQPTLNYAGI EQAQIVVEAV VENPKIKAAV LSETETLVNE 

       430        440        450        460        470        480 
DCVLASNTST IPISELAKSL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS EKTISTVVAY 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLLPYLLGF GLLLRDGGDF RQIDKIMEKE FGWPMGPAYL 

       550        560        570        580        590        600 
IDVIGLDTAH HSQSVMAQGF PDRMHRDYKD AIHVLYDNQR YGQKNGLGFY KYTQDKKGKP 

       610        620        630        640        650        660 
KKEQDEQTDQ LLATICQQKS NFSGEEIIAR TMIPMINEVV RCLEEGVIAS PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG VFRYLETMGT AAYVKMAENY AHLGALYQVP PGLKAKAERN ESYYSTAATI 


AVSTGKTA

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References

[1]

"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens."
Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K.

Kunst F.
Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TT01.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571873 Genomic DNA. Translation: CAE16774.1.
RefSeq	NP_931575.1.
3D structure databases
SMR	Q7MZ92. Positions 1-715.
ModBase	Search...
Genome annotation databases
GeneID	2804423.
KEGG	plu:plu4402.
NMPDR	fig\|243265.1.peg.4198.
Organism-specific databases
PhotoList	plu4402.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG691737.
OMA	YFGGFAR.
Enzyme and pathway databases
BioCyc	PLUM243265:PLU4402-MONOMER.
BRENDA	1.1.1.35. 308689. 4.2.1.17. 308689. 5.1.2.3. 308689. 5.3.3.8. 308689.
Family and domain databases
HAMAP	MF_01621. FadB. [Tree]
InterPro	IPR006180. 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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
Pfam	PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
TIGRFAMs	TIGR02437. FadB. 1 hit.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

FADB_PHOLL

Accession

Primary (citable) accession number: Q7MZ92

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 15, 2003
Last modified:	February 9, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (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)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents