Reviewed, UniProtKB/Swiss-Prot A8FP63 (FADB_SHESH)

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:	Ssed_0023

Organism

Shewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]

Taxonomic identifier

425104 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	716 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
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.
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.

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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 716	716	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_1000088085
Regions
	Region	1 – 189	189	Enoyl-CoA hydratase/isomerase By similarity
	Region	311 – 716	406	3-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8FP63-1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: AD91C405CB10CF8A	FASTA	716	77,021
	10 20 30 40 50 60 MIYQSPTIQV ELLEDNIARL CFNASGSVNK LDRETINSLD AALDAIQQDS HIQALVLTSA 70 80 90 100 110 120 KGAFIVGADI TEFLGLFAQE DSVLLPWIAE ANVVFNKLED LPFPTISAIN GFALGGGFET 130 140 150 160 170 180 VLATDFRIAD TTAKIGLPET KLGLIPGFGG TVRLPRLIGT DNALEWITSG KDQRPEAALK 190 200 210 220 230 240 VGAIDAVVAP ENLQASAIKM LKDALAEKLD WQSRRARKQA ALTLPKLEAM MSFATAKGMV 250 260 270 280 290 300 FKIAGKHYPA PMAAISVIEQ AARCGRADAL KVEHQAFVKL AKTDVAQALI GIFLNDQLVK 310 320 330 340 350 360 GKAKKAGKLA KNIDTAAVLG AGIMGGGIAY QSASKGTPII MKDIAQPALE LGLGEASKLL 370 380 390 400 410 420 AAQIKRGRST PQKMAKVLNN ITATLDYTPV KDVDVVVEAV VEHPKVKSMV LAEVEQNVSD 430 440 450 460 470 480 DAIITSNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEVIRGENSS EETIASVVAY 490 500 510 520 530 540 ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLADGADF AAIDKVMEKQ FGWPMGPAYL 550 560 570 580 590 600 LDVVGIDTGH HAQAVMAEGF PDRMGKNGKD AIDIMFEAER FGQKNSKGFY AYSVDRRGKP 610 620 630 640 650 660 KKDVDPTSYE LLGAEFGELK AFESEDIIAR TMIPMIIETV RCLEEGIIAT PAEADMGLVF 670 680 690 700 710 GLGFPPFRGG VFRYIDTMGV ANFVALADKY AHLGGLYQVT DAMRELAANN GSYYQS

References

[1]

"Complete sequence of Shewanella sediminis HAW-EB3." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Zhao J.-S., Richardson P. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000821 Genomic DNA. Translation: ABV34636.1.
RefSeq	YP_001471764.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5612855.
GenomeReviews	Gene locus Ssed_0023 in contig CP000821_GR.
KEGG	sse:Ssed_0023.
NMPDR	fig|425104.3.peg.20.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A8FP63. ANNGSYY.
Family and domain databases
HAMAP	MF_01621. [Tree]
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. 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. 1 hit. 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...

Entry information

Entry name

FADB_SHESH

Accession

Primary (citable) accession number: A8FP63

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	November 13, 2007
Last modified:	June 16, 2009
This is version 14 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)