Bifunctional protein aas - Erwinia carotovora subsp. atroseptica

Preferred order of sections

Names and origin

Protein names

Recommended name:
Bifunctional protein aas

Including the following 2 domains:

2-acylglycerophosphoethanolamine acyltransferase
EC=2.3.1.40
Alternative name(s):
2-acyl-GPE acyltransferase
Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
Acyl-[acyl-carrier-protein] synthetase
EC=6.2.1.20
Alternative name(s):
Acyl-ACP synthetase
Long-chain-fatty-acid--[acyl-carrier-protein] ligase

Gene names

Name:	aas
Ordered Locus Names:	ECA3641

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1 By similarity. HAMAP MF_01162
Catalytic activity	Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine. HAMAP MF_01162 ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein]. HAMAP MF_01162
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_01162.
Sequence similarities	In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Acyltransferase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: InterPro phospholipid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity Inferred from electronic annotation. Source: EC long-chain fatty acid [acyl-carrier-protein] ligase 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 – 738

738

Bifunctional protein aas HAMAP MF_01162

PRO_0000193049

Regions

Transmembrane

258 – 277

20

Helical; Potential

Transmembrane

409 – 433

25

Helical; Potential

Region

15 – 138

124

Acyltransferase HAMAP MF_01162

Region

233 – 646

414

AMP-binding HAMAP MF_01162

Sites

Active site

36

1

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6D107 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 814D20817360FCF8
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FASTA

738

81,428

        10         20         30         40         50         60 
MIHTLLRWVF QRLYRIRIEG DSSQFQQSKL LITPNHVSFL DGVLLALFLP IKPVFAVYSS 

        70         80         90        100        110        120 
ISDRWFMRWL KPYIDFVPLD PTKPLAIKGL IKVIERGQPV VVFPEGRISV TGSLMKVYSG 

       130        140        150        160        170        180 
AAFVAAKSGA TIIPVRIDGI ELSPFGRLAG VFKRRCLPQV TITYLPPTTL PMPEASSARA 

       190        200        210        220        230        240 
RRALAGERLH QIMMKARMET RPQHTLYQAF LAARSRYGRH SASIADISFN EDSYQGLLKK 

       250        260        270        280        290        300 
SLGVSRILQR FTRADEHVGM LLPNATITAA SILGASLRNR IPAMLNYTAG AKGLQSAMKA 

       310        320        330        340        350        360 
AGIKTIVTSR QFLEKGKLTD LPKQVSEANW VYLEDLKDTV TLKDKLWILF HLLFPARAML 

       370        380        390        400        410        420 
PQKPDDAAIV LFTSGSEGNP KGVVHSHDSL LANVEQIRTV ADFTPGDRFM SALPLFHAFG 

       430        440        450        460        470        480 
LTVGLLTPLI TGARVFLYPS PLHYRIVPEL VYDQNCTVLF GTSTFLGNYA RFAHPYDFAR 

       490        500        510        520        530        540 
LRYVVAGAEK LSETTRQVWQ DKFGIRILEG YGVTECAPVV AINVPMATKI HSVGLLLPEM 

       550        560        570        580        590        600 
ESRLITVPGI TRGGRLQLRG PNIMKGYLRV ENPGVLETPA AENAEGELQQ GWYDTGDIVE 

       610        620        630        640        650        660 
LDERGFCTII GRVKRFAKLA GEMVSLESVE QLAVKVSPEA QHAASAKSDS SKGEALVLFT 

       670        680        690        700        710        720 
TDSQITRDVL LAQARSSGVP ELAVPRDIRY VKALPLLGSG KPDFVTLRQM AEEPNSEQSV 

       730 
IEPSIVKQPI TNASEPSA

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References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors."
Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.

Toth I.K.
Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950851 Genomic DNA. Translation: CAG76539.1.
RefSeq	YP_051729.1. NC_004547.2.
3D structure databases
ProteinModelPortal	Q6D107.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2885271.
GenomeReviews	Gene locus ECA3641 in contig BX950851_GR.
KEGG	eca:ECA3641.
NMPDR	fig\|218491.3.peg.2243.
PATRIC	20482681. VBIPecAtr54885_3694.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG361068.
OMA	ANWVYLE.
ProtClustDB	PRK08043.
Enzyme and pathway databases
BioCyc	ECAR218491:ECA3641-MONOMER.
Family and domain databases
HAMAP	MF_01162. Aas. [Tree]
InterPro	IPR002123. Acyltransferase. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR023775. Bifunctional_Aas. [Graphical view]
KO	K05939.
Pfam	PF01553. Acyltransferase. 1 hit. PF00501. AMP-binding. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAS_ERWCT

Accession

Primary (citable) accession number: Q6D107

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents