Reviewed, UniProtKB/Swiss-Prot Q489W3 (FADB_COLP3)

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:	CPS_0393

Organism

Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]

Taxonomic identifier

167879 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Colwelliaceae › Colwellia

Protein attributes

Sequence length	722 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 – 722	722	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_0000109265
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 – 722	412	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)
	Q489W3-1 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: A174E51D6CB6A318	FASTA	722	77,146
	10 20 30 40 50 60 MIYQGKSLSA QLLEDGIVEF KFDAQGSVNK FDQATFEEYI AVVAAINNCS EAKGVIVTSG 70 80 90 100 110 120 KSTFIVGADI TEFLVSFSQP EDALASWAKK ASDVFDSFED IQLPTIAAIN GIALGGGCEM 130 140 150 160 170 180 TLACDYRVAA TTASIGLPEV KLGLMPGFGG TVRLPRLIGF DNAATWMSTG KAFKPAAALA 190 200 210 220 230 240 QGAIDAVVEP ENLQAAAISM LKLAIDGKLD WRAKRQPKLE ALKLSPTELI MSSTTCKGMI 250 260 270 280 290 300 AAKAGKHYPA PMVMINTLIA SANLDRTGAM AAENTGFAKL AKTDAATAQI GLFMADQVIK 310 320 330 340 350 360 GKAKKASKLA TKAVNKAAVL GAGIMGGGIA YQSAYKGTPI IMKDINDQAL DLGLTTATGI 370 380 390 400 410 420 LTKQVERGRM NAKKMAGVLN NITPSLSYDS VKDVDIVVEA VVENPKVKGM VLAEVEGVIG 430 440 450 460 470 480 EDAILTSNTS TISIDLLAQS VKRPQNFCGM HFFNPVNKMP LVEVIRGKDT SDETVAAVVA 490 500 510 520 530 540 YAAKMGKSPI VVNDCPGFYV NRVLFPYFAG FSQLVLEGAD FTAIDKVMEK QFGWPMGPAY 550 560 570 580 590 600 LLDVVGVDTA DHCTGVMSSG FPTRMKKIDN DPVSTLYANE RLGQKNGKGF YDHIKDKRGR 610 620 630 640 650 660 PMKVPAPVAY ELLGQHCADK KDFSSEEIIA RMMIPMVNEV VRCLEEGVVD TAAEADMGLI 670 680 690 700 710 720 YGVGFPPFRG GAIRYLETLG LDNFIAMADK YTDLGEIYHV TDGLREMAKS GKSYFTTDVK LA

References

[1]

"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses." Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000083 Genomic DNA. Translation: AAZ26244.1.
RefSeq	YP_267151.1.
3D structure databases
SMR	Q489W3. Positions 1-715.
ModBase	Search...
Protein-protein interaction databases
STRING	Q489W3.
Genome annotation databases
GeneID	3520494.
GenomeReviews	Gene locus CPS_0393 in contig CP000083_GR.
KEGG	cps:CPS_0393.
NMPDR	fig|167879.3.peg.451.
TIGR	CPS_0393.
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HBG691737.
OMA	YFGGFAR.
Enzyme and pathway databases
BioCyc	CPSY167879:CPS_0393-MONOMER.
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. 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_COLP3

Accession

Primary (citable) accession number: Q489W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	September 13, 2005
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)