Reviewed, UniProtKB/Swiss-Prot A6VVM8 (FADA_MARMS)

Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase
    EC=2.3.1.16
Alternative name(s):
    Fatty acid oxidation complex subunit beta
    Beta-ketothiolase
    Acetyl-CoA acyltransferase

Gene names

Name:	fadA
Ordered Locus Names:	Mmwyl1_1579

Organism

Marinomonas sp. (strain MWYL1) [Complete proteome] [HAMAP]

Taxonomic identifier

400668 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Marinomonas

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. HAMAP MF_01620
Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. HAMAP MF_01620
Subcellular location	Cytoplasm By similarity HAMAP MF_01620.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: HAMAP lipid catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase 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 – 391	391	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_1000088078
Sites
	Active site	95	1	Acyl-thioester intermediate By similarity
	Active site	347	1	Proton acceptor By similarity
	Active site	377	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6VVM8-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 702052532C439974	FASTA	391	41,225
	10 20 30 40 50 60 MKLNPNDVVI IDAVRSPMGK TKNGVFRNVR AENLSAALVK ELFKRNPNVD QKDVEDLIWG 70 80 90 100 110 120 CVNQTLEQGF NMARAVSLLA GLPITCAAQT VNRLCGSSMS AIHTAAQAIM TGQGDVFVVG 130 140 150 160 170 180 GVEHMGHVGM MHGVDVNPAL SKHMAKASMM MGVTAEMLGK MHGVSREDQD AFAVRSHRLA 190 200 210 220 230 240 HEATLQGRFN NEIVSIEGHD ADGNKILVEV DEVIRPETSM ESLAKLAPVF MPKVGTVTAG 250 260 270 280 290 300 TSSALSDGAS AMLMMSAKKA EELGLTPIAK VRSMAVAGCD PAIMGYGPVP ATKKALKRAG 310 320 330 340 350 360 LTIADIDIVE LNEAFAAQSI PVLKDLGLLD LVDDKVNLNG GAIALGHPLG CSGTRISTTL 370 380 390 LNVMREKDAT VGLATMCIGM GQGIATVFER V

References

[1]

"Complete sequence of Marinomonas sp. MWYL1." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000749 Genomic DNA. Translation: ABR70507.1.
RefSeq	YP_001340442.1.
3D structure databases
SMR	A6VVM8. Positions 3-391.
ModBase	Search...
Protein-protein interaction databases
STRING	A6VVM8.
Genome annotation databases
GeneID	5367331.
GenomeReviews	Gene locus Mmwyl1_1579 in contig CP000749_GR.
KEGG	mmw:Mmwyl1_1579.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	AIDDIYW.
Family and domain databases
HAMAP	MF_01620. FadA. [Tree]
InterPro	IPR012805. FadA. IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020610. Thiolase_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit. TIGR02445. fadA. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADA_MARMS

Accession

Primary (citable) accession number: A6VVM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	August 21, 2007
Last modified:	February 9, 2010
This is version 24 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)