Reviewed, UniProtKB/Swiss-Prot Q9KNI1 (FADB_VIBCH)

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:	VC_2758

Organism

Vibrio cholerae [Complete proteome] [HAMAP]

Taxonomic identifier

666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
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. 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.

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_0000255846
Regions
	Nucleotide binding	401 – 403	3	NAD By similarity
	Nucleotide binding	428 – 430	3	NAD By similarity
	Region	1 – 189	189	Enoyl-CoA hydratase/isomerase By similarity
	Region	311 – 723	413	3-hydroxyacyl-CoA dehydrogenase By similarity
Sites
	Binding site	296	1	Substrate By similarity
	Binding site	325	1	NAD; via amide nitrogen By similarity
	Binding site	344	1	NAD By similarity
	Binding site	408	1	NAD By similarity
	Binding site	454	1	NAD By similarity
	Binding site	501	1	Substrate By similarity
	Binding site	661	1	Substrate By similarity
	Site	119	1	Important for catalytic activity By similarity
	Site	139	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KNI1-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 147F5ABD0B0797F8	FASTA	723	78,108
	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

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF95897.1.
PIR	H82035.
RefSeq	NP_232384.1.
3D structure databases
HSSP	HSSP built from PDB template 1WDL based on UniProtKB P28793.
SMR	Q9KNI1. Positions 1-716.
ModBase	Search...
Genome annotation databases
GeneID	2614935.
GenomeReviews	Gene locus VC_2758 in contig AE003852_GR.
KEGG	vch:VC2758.
TIGR	VC_2758.
Phylogenomic databases
HOGENOM	HBG691737.
OMA	YFGGFAR.
Enzyme and pathway databases
BRENDA	1.1.1.35. 19019. 4.2.1.17. 19019. 5.1.2.3. 19019. 5.3.3.8. 19019.
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. 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. 2 hits.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADB_VIBCH

Accession

Primary (citable) accession number: Q9KNI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 55 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)