Reviewed, UniProtKB/Swiss-Prot Q0I0T3 (FADB_SHESR)

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:	Shewmr7_0016

Organism

Shewanella sp. (strain MR-7) [Complete proteome] [HAMAP]

Taxonomic identifier

60481 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	716 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 – 716	716	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_1000069580
Regions
	Nucleotide binding	400 – 402	3	NAD By similarity
	Nucleotide binding	427 – 429	3	NAD By similarity
	Region	1 – 189	189	Enoyl-CoA hydratase/isomerase By similarity
	Region	311 – 716	406	3-hydroxyacyl-CoA dehydrogenase By similarity
Sites
	Binding site	296	1	Substrate By similarity
	Binding site	324	1	NAD; via amide nitrogen By similarity
	Binding site	343	1	NAD By similarity
	Binding site	407	1	NAD By similarity
	Binding site	453	1	NAD By similarity
	Binding site	500	1	Substrate By similarity
	Binding site	660	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)
	Q0I0T3-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 818A76A7B7C7C25D	FASTA	716	76,641
	10 20 30 40 50 60 MIYQSPTIQV ELLEDNIAKL CFNAPGSVNK FDRETLASLD AALDSIKQQS NIQALVLTSG 70 80 90 100 110 120 KDTFIVGADI TEFLGLFAQD DAVLLSWVEQ ANAVFNKLED LPFPTASAIK GFALGGGCET 130 140 150 160 170 180 ILATDFRIAD TTAKIGLPET KLGIIPGFGG TVRLPRVIGA DNALEWITTG KDQRPEDALK 190 200 210 220 230 240 VGAVDAVVAP EALEAAAIQM LKDAVAEKLD WQARRHRKMS PLTLPKLEAM MSFTTAKGMV 250 260 270 280 290 300 FAVAGKHYPA PMAAVSVVEQ AATKGRSDAL QIEHQAFIKL AKTDVAKALI GIFLNDQLVK 310 320 330 340 350 360 GKAKKAGKLA KDVKSAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALD LGLGEAAKLL 370 380 390 400 410 420 SAQVARGRST PEKMAKVLNN ITPALDYAPV NHADVVVEAV VEHPKVKAQV LAEVEQYVSE 430 440 450 460 470 480 DAIIASNTST ISINLLAKSM KKPERFCGMH FFNPVHKMPL VEVIRGEHSS EETIASVVAY 490 500 510 520 530 540 ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF NGLLAEGGDF AAIDKVMEKQ FGWPMGPAYL 550 560 570 580 590 600 LDVVGLDTGH HAQAVMAEGF PDRMGKSGND AIDVMFENKR LGQKNGKGFY AYSVDSRGKP 610 620 630 640 650 660 KKDVDPTSYE LLKAAFGEQK AFDADEIIAR TMIPMIIETV RCLEEGIVAS PAEADMGLVY 670 680 690 700 710 GLGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT DAMRALAANN GSYYQA

References

[1]

"Complete sequence of chromosome 1 of Shewanella sp. MR-7." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000444 Genomic DNA. Translation: ABI41022.1.
RefSeq	YP_736079.1.
3D structure databases
SMR	Q0I0T3. Positions 1-714.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0I0T3.
Genome annotation databases
GeneID	4258049.
GenomeReviews	Gene locus Shewmr7_0016 in contig CP000444_GR.
KEGG	shm:Shewmr7_0016.
NMPDR	fig|60481.10.peg.16.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HBG691737.
OMA	ASRFGQK.
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. 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_SHESR

Accession

Primary (citable) accession number: Q0I0T3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 3, 2006
Last modified:	February 9, 2010
This is version 35 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)