Reviewed, UniProtKB/Swiss-Prot Q8ZAN0 (FADB_YERPE)

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:	YPO3766, y0464, YP_3282

Organism

Yersinia pestis [Complete proteome] [HAMAP]

Taxonomic identifier

632 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

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_0000109295
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)
	Q8ZAN0-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 2C534B2963B09491	FASTA	729	78,826
	10 20 30 40 50 60 MLYQSETLQL HWLENGIAEL VFDAPGSVNK LDTKTVANLG EALNVLEKQS ELKGLLLRSA 70 80 90 100 110 120 KTALIVGADI TEFLSLFNAP PEKLHQWLVF ANTIFNRLED LPVPTISAIN GYALGGGCEC 130 140 150 160 170 180 ILATDFRIAS PEARIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIATG KDVTANDALK 190 200 210 220 230 240 IGLVDAVVDP EKLVGSALTM LKQAIDGKLD WQAARRPKLE PLKLNPTEAA MCFTIAKGRV 250 260 270 280 290 300 MQVAGKHYPA PLTAVKTIEA AAKFGRTEAL NLETNSFVPL AGSNEARALV GIFLNDQYVK 310 320 330 340 350 360 AQAKKLSKGV AAPKLAAVLG AGIMGGGIAY QSALKSVPVI MKDINENSLD LGMNEAAKLL 370 380 390 400 410 420 NKQLERGKVD GLKMASILAT IRPTLDYAGI ERAQVIVEAV VENPKVKAAV LAEVEALIGE 430 440 450 460 470 480 DTVLASNTST IPIDQLAKSL KRPENFCGMH FFNPVHRMPL VEIIRGAKTS DKTLAAVVAY 490 500 510 520 530 540 ATQMGKTPIV VNDCPGFFVN RVLFPYLAGF GMLVRDGGDF HQIDKVMEKQ FGWPMGPAYL 550 560 570 580 590 600 LDVVGIDTAH HAQAVMAAGF PERMNKDYRD AVDVMFDNQR FGQKNGQGFY RYTQDAKGKP 610 620 630 640 650 660 RKENDEQVDK LLAEISQPLQ EFSDEDIIAR TMIPMINEVV RCLEEGIIAS AAEGDMALVY 670 680 690 700 710 720 GLGFPPFHGG VFRYLDTLGS ANYVEMAQRY AHLGALYHVP AGLRAKAEHN ESYYPVAAAL LDVSTNQPA

References

[1]	"Genome sequence of Yersinia pestis, the causative agent of plague." Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:523-527(2001) [PubMed: 11586360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CO-92 / Biovar Orientalis.
[2]	"Genome sequence of Yersinia pestis KIM." Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. , Matson J.S., Blattner F.R., Perry R.D. J. Bacteriol. 184:4601-4611(2002) [PubMed: 12142430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KIM5 / Biovar Mediaevalis.
[3]	"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans." Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R. DNA Res. 11:179-197(2004) [PubMed: 15368893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL590842 Genomic DNA. Translation: CAL22353.1. AE009952 Genomic DNA. Translation: AAM84053.1. AE017042 Genomic DNA. Translation: AAS63449.1.
PIR	AF0458.
RefSeq	NP_667802.1. NP_994572.1. YP_002348645.1.
3D structure databases
HSSP	HSSP built from PDB template 3HDH based on UniProtKB P00348.
ModBase	Search...
Genome annotation databases
GeneID	1145411. 1176601. 2764613.
GenomeReviews	Gene locus y0464 in contig AE009952_GR. Gene locus YP_3282 in contig AE017042_GR. Gene locus YPO3766 in contig AL590842_GR.
KEGG	ype:YPO3766. ypk:y0464. ypm:YP_3282.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8ZAN0.
OMA	Q8ZAN0. ANNGSYY.
Enzyme and pathway databases
BioCyc	YPES187410:Y0464-MON. YPES214092:YPO3766-MON. YPES229193:YP3282-MON.
BRENDA	1.1.1.35. 142588. 4.2.1.17. 142588. 5.1.2.3. 142588. 5.3.3.8. 142588.
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_YERPE

Accession

Primary (citable) accession number: Q8ZAN0
Secondary accession number(s): Q0WAP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 66 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)