Reviewed, UniProtKB/Swiss-Prot Q8Z3C6 (FADB_SALTI)

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:	STY3577, t3315

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	729 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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids 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 – 729	729	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_0000109286
Regions
	Region	1 – 189	189	Enoyl-CoA hydratase/isomerase By similarity
	Region	311 – 729	419	3-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Z3C6-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: C34C68ECFF35713C	FASTA	729	79,642
	10 20 30 40 50 60 MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG QALEVLEKQH DLKGLLLRSN 70 80 90 100 110 120 KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTLAAVN GYALGGGCEC 130 140 150 160 170 180 VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRLPRMLGA DSALEIIAAG KDVGAEHALK 190 200 210 220 230 240 IGLVDGVVKQ EKLIEGAIAV LRQAITGDLD WRAKRQPKLE PLKLSKIEAA MSFTIAKGMV 250 260 270 280 290 300 AQTAGKHYPA PMTAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 310 320 330 340 350 360 GKAKKLTKDI ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLN LGMTEAAKLL 370 380 390 400 410 420 NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRP 430 440 450 460 470 480 ETVLASNTST IPIGELASAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW 490 500 510 520 530 540 ASKMGKTPIV VNNCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL 550 560 570 580 590 600 LDVVGIDTAH HAQAVMAAGF PQRMQKEYRD AIDALFDASR FGQKNGLGFW RYKEDSKGKP 610 620 630 640 650 660 KKEEDAAVDD LLASVSQTKR DFSDDEIIAR MMIPMINEVV RCLEEGIIAS PAEADMALVY 670 680 690 700 710 720 GLGFPPFHGG AFRWLDTQGS AKYLDMAQQY QHLGPLYEVP EGLRDKTRHN EPYYPPVEPA RPVGSLKTA

References

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL627278 Genomic DNA. Translation: CAD07910.1. AE014613 Genomic DNA. Translation: AAO70843.1.
RefSeq	NP_457769.1. NP_806983.1.
3D structure databases
HSSP	HSSP built from PDB template 1F0Y based on UniProtKB Q16836.
ModBase	Search...
Genome annotation databases
GeneID	1071579. 1249832.
GenomeReviews	Gene locus t3315 in contig AE014613_GR. Gene locus STY3577 in contig AL513382_GR.
KEGG	stt:t3315. sty:STY3577.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8Z3C6.
OMA	Q8Z3C6. ANNGSYY.
Enzyme and pathway databases
BioCyc	SENT209261:T3315-MON. SENT220341:STY3577-MON.
BRENDA	1.1.1.35. 3716. 4.2.1.17. 3716. 5.1.2.3. 3716. 5.3.3.8. 3716.
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. 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...

Entry information

Entry name

FADB_SALTI

Accession

Primary (citable) accession number: Q8Z3C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 54 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)