Reviewed, UniProtKB/Swiss-Prot A1S1I8 (FADB_SHEAM)

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:	Sama_0032

Organism

Shewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP]

Taxonomic identifier

326297 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	716 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 – 716	716	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_1000069572
Regions
	Region	1 – 188	188	Enoyl-CoA hydratase/isomerase By similarity
	Region	310 – 716	407	3-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1S1I8-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 93251CB6B0C3D409	FASTA	716	76,369
	10 20 30 40 50 60 MIYQSPTIQV ELTADKIARL CFNAPGSVNK FDRETLASLN AALDVLKDSD AKAAVLTSGK 70 80 90 100 110 120 DTFIVGADIT EFLALFAEED AKLMEWIAQA NVVFNKLEDL PFPTVSAIKG FALGGGCEAI 130 140 150 160 170 180 LATDFRVADT SAKIGLPETK LGLIPGFGGT VRLPRLIGAD NALEWITTGK DQRPEDALKV 190 200 210 220 230 240 GAIDAVVAPE NLEAAAIQML NDALAGKLDW QARRARKQAP LTLPKLEAMM SFTTAKGMVY 250 260 270 280 290 300 AVAGKHYPAP MAAVSVVEQA AGMSRAEALV VEHNAFIKLA KTDVATALIG IFLNDQLVKG 310 320 330 340 350 360 KAKKASKLAK DIKHAAVLGA GIMGGGIAYQ SASKGTPIVM KDINQAALDL GVNEAAKLLS 370 380 390 400 410 420 AQVARGRSTP DKMAKVLNNI TPALDYAPLK DVNVVVEAVV ENPKVKAMVL ADVENVVADD 430 440 450 460 470 480 AIIASNTSTI SIDLLAKSLK NPARFCGMHF FNPVHKMPLV EVIRGKDTSE ETVASVVAYA 490 500 510 520 530 540 SKMGKTPIVV NDCPGFFVNR VLFPYFAGFN GLLADGGDFA AIDKVMEKQF GWPMGPAYLL 550 560 570 580 590 600 DVVGLDTGHH AQAVMADGFP DRMGKSDKDA IDVMYEAGRL GQKNGKGFYQ YSIDKRGKPK 610 620 630 640 650 660 KDVDPASYTM LAEAFGAQKA FEADEIIART MIPMIIETVR CLEEGIVASP AEADMGLVYG 670 680 690 700 710 LGFPPFRGGV FRYLDTMGVA NFVALADKYA HLGGLYQVTD AMRELASNNG SYYPKA

References

[1]

"Complete sequence of Shewanella amazonensis SB2B." 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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000507 Genomic DNA. Translation: ABL98244.1.
RefSeq	YP_925914.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4602289.
GenomeReviews	Gene locus Sama_0032 in contig CP000507_GR.
KEGG	saz:Sama_0032.
NMPDR	fig|326297.7.peg.28.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A1S1I8. ANNGSYY.
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_SHEAM

Accession

Primary (citable) accession number: A1S1I8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 22 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)