Reviewed, UniProtKB/Swiss-Prot A7N1D2 (FADB_VIBHB)

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:	VIBHAR_00460

Organism

Vibrio harveyi (strain ATCC BAA-1116 / BB120) [Complete proteome] [HAMAP]

Taxonomic identifier

338187 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	723 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 – 723	723	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_1000069583
Regions
	Region	1 – 189	189	Enoyl-CoA hydratase/isomerase By similarity
	Region	312 – 723	412	3-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7N1D2-1 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: F9A6F1B919EF479D	FASTA	723	78,649
	10 20 30 40 50 60 MIYQAETLQV KEVQDGIAEL SFCSPKSVNK LDLATLESLD KALDALKAHQ GLKGLMLTSD 70 80 90 100 110 120 KDAFIVGADI TEFLGLFAKT DAELDQWLQF ANSIFNKLED LPVPTISVLK GHTLGGGCEC 130 140 150 160 170 180 VLATDMRIGD KTTSIGLPET KLGIMPGFGG CVRLPRVIGA DSAMEVITQG KACRADEALK 190 200 210 220 230 240 IGLLDAVVDS DALYESALKT LTSAINEKLD WQARRKQKTS PLTLSKLESM MSFTMAKGLV 250 260 270 280 290 300 AQKAGPHYPA PMTAVITIEE GARFARNEAL DIERKHFVKL AKSEEAKSLV GLFLNDQYIK 310 320 330 340 350 360 GLAKKSAKSA SKDTQRAAVL GAGIMGGGIA YQSALKGVPV LMKDIAQPSL DLGMTEASKL 370 380 390 400 410 420 LNKRLSRGRI DGFKMAGILA SITPSLHYTG IEESDVIVEA VVENPKVKAA VLSEVESHVG 430 440 450 460 470 480 EDTVITSNTS TIPINLLAKS LKRPENFCGM HFFNPVHRMP LVEIIRGEHT SDETINRVVA 490 500 510 520 530 540 YAAKMGKSPI VVNDCPGFFV NRVLFPYFGG FSMLLRDGAD FTKIDKIMER KFGWPMGPAY 550 560 570 580 590 600 LLDVVGIDTA HHAQAVMAQG FPERMGKQGR DAIDALFEAS KYGQKNGSGF YSYTIDRKGK 610 620 630 640 650 660 PKKTFSEEIL PVLADVCTDK QDFDDQTIIQ RMMIPMINEV VLCLQEGIIA TPQEADMTLV 670 680 690 700 710 720 YGLGFPPFRG GVFRYLDSVG IAEFVAMAKQ YSELGAMYQV PQMLIDMAAK GESFYGAQQQ GSI

References

[1]

Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C., Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J., Wilson R.K. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000789 Genomic DNA. Translation: ABU69475.1.
RefSeq	YP_001443702.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5552832.
GenomeReviews	Gene locus VIBHAR_00460 in contig CP000789_GR.
KEGG	vha:VIBHAR_00460.
NMPDR	fig|338187.4.peg.356.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A7N1D2. QFANSIF.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADB_VIBHB

Accession

Primary (citable) accession number: A7N1D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 2, 2007
Last modified:	June 16, 2009
This is version 16 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)