A1TZR8 (FADA_MARAV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-ketoacyl-CoA thiolase
EC=2.3.1.16

Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta

Gene names

Name:	fadA
Ordered Locus Names:	Maqu_1145

Organism

Marinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845)) [Complete proteome] [HAMAP]

Taxonomic identifier

351348 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Marinobacter

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.
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: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC
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_0000292892
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)
	A1TZR8 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 4F41504DAF44E782	FASTA	391	41,807
	10 20 30 40 50 60 MSLNPRDVVV VDCVRTPMGR AKNGCFRNVR AETLSAALIE ALFERNPKLD PKEVEDVIWG 70 80 90 100 110 120 CVNQTKEQGF NVARQISLLT RIPHESAAQT VNRLCGSAMS AIHTAAQAIQ TGNGDVFLVG 130 140 150 160 170 180 GVEHMGHVPM TEGFDHNPAA SKYSAKASNM MGLTAEMLAK MHGITREQQD EFGARSHRLA 190 200 210 220 230 240 HEATQEGRFK NEIVPIEGHD ENGFVKLIEE DETIRPETTA ESLGQLRPAF DPKNGTVTAG 250 260 270 280 290 300 TSSQLTDGAS AMVLMSAERA EALGLTPIAK IRSMAVAGCD PAIMGYGPVP ATKKALKRAG 310 320 330 340 350 360 LKVEDIDFWE LNEAFAGQSL PVLKDLKLLG VMEEKVNLNG GAIALGHPLG CSGARISTTL 370 380 390 LNIMQAKGGK LGVSTMCIGL GQGIATVWER I

References

[1]

"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8." 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., Kim E., Edwards K., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000514 Genomic DNA. Translation: ABM18237.1.
RefSeq	YP_958424.1. NC_008740.1.
3D structure databases
ProteinModelPortal	A1TZR8.
SMR	A1TZR8. Positions 2-391.
ModBase	Search...
Protein-protein interaction databases
STRING	A1TZR8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4654319.
GenomeReviews	Gene locus Maqu_1145 in contig CP000514_GR.
KEGG	maq:Maqu_1145.
PATRIC	22457542. VBIMarAqu65105_1544.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	AIDDIYW.
PhylomeDB	A1TZR8.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	MAQU351348:MAQU_1145-MONOMER.
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. 4 hits.
KO	K00632.
PANTHER	PTHR18919:SF35. PTHR18919:SF35. 1 hit. 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.
SUPFAM	SSF53901. Thiolase-like. 2 hits.
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_MARAV

Accession

Primary (citable) accession number: A1TZR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	February 6, 2007
Last modified:	December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program