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Bifunctional protein Aas [Includes: 2-acylglycerophosphoethanolamine acyltransferase (EC 2.3.1.40) (2-acyl-GPE acyltransferase) (Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase); Acyl-[acyl-carrier-protein] synthetase (EC 6.2.1.20) (Acyl-ACP synthetase) (Long-chain-fatty-acid--[acyl-carrier-protein] ligase)]

 AAS_ECOLI               Reviewed;         719 AA.
P31119; Q2MA01; Q46935; Q6IU49;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
30-AUG-2017, entry version 139.
RecName: Full=Bifunctional protein Aas {ECO:0000255|HAMAP-Rule:MF_01162};
Includes:
RecName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
EC=2.3.1.40 {ECO:0000255|HAMAP-Rule:MF_01162};
AltName: Full=2-acyl-GPE acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
Includes:
RecName: Full=Acyl-[acyl-carrier-protein] synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
EC=6.2.1.20 {ECO:0000255|HAMAP-Rule:MF_01162};
AltName: Full=Acyl-ACP synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase {ECO:0000255|HAMAP-Rule:MF_01162};
Name=aas {ECO:0000255|HAMAP-Rule:MF_01162};
OrderedLocusNames=b2836, JW2804;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8300626;
Jackowski S., Jackson P.D., Rock C.O.;
"Sequence and function of the aas gene in Escherichia coli.";
J. Biol. Chem. 269:2921-2928(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-311.
STRAIN=B / Bc251;
PubMed=12664169; DOI=10.1007/s00239-002-2423-0;
Lenski R.E., Winkworth C.L., Riley M.A.;
"Rates of DNA sequence evolution in experimental populations of
Escherichia coli during 20,000 generations.";
J. Mol. Evol. 56:498-508(2003).
[5]
FUNCTION.
STRAIN=K12;
PubMed=1649829;
Hsu L., Jackowski S., Rock C.O.;
"Isolation and characterization of Escherichia coli K-12 mutants
lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and
acyl-acyl carrier protein synthetase activity.";
J. Biol. Chem. 266:13783-13788(1991).
[6]
MUTAGENESIS OF HIS-36.
STRAIN=K12;
PubMed=9515909;
Heath R.J., Rock C.O.;
"A conserved histidine is essential for glycerolipid acyltransferase
catalysis.";
J. Bacteriol. 180:1425-1430(1998).
-!- 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.
{ECO:0000255|HAMAP-Rule:MF_01162, ECO:0000269|PubMed:1649829}.
-!- 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.
{ECO:0000255|HAMAP-Rule:MF_01162}.
-!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + an [acyl-
carrier-protein] = AMP + diphosphate + a long-chain acyl-[acyl-
carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_01162}.
-!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
protein.
-!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
acetyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01162}.
-!- SIMILARITY: In the C-terminal section; belongs to the ATP-
dependent AMP-binding enzyme family. {ECO:0000255|HAMAP-
Rule:MF_01162}.
-----------------------------------------------------------------------
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EMBL; L14681; AAA17550.1; -; Unassigned_DNA.
EMBL; U29581; AAB40483.1; -; Genomic_DNA.
EMBL; U00096; AAC75875.1; -; Genomic_DNA.
EMBL; AP009048; BAE76905.1; -; Genomic_DNA.
EMBL; AY625100; AAT42454.1; -; Genomic_DNA.
PIR; E65066; E65066.
RefSeq; NP_417313.1; NC_000913.3.
RefSeq; WP_000899054.1; NZ_LN832404.1.
ProteinModelPortal; P31119; -.
BioGrid; 4259527; 15.
DIP; DIP-9025N; -.
IntAct; P31119; 9.
MINT; MINT-1308806; -.
STRING; 316385.ECDH10B_3006; -.
TCDB; 4.C.1.1.16; the fatty acid transporter (fat) family.
PaxDb; P31119; -.
PRIDE; P31119; -.
EnsemblBacteria; AAC75875; AAC75875; b2836.
EnsemblBacteria; BAE76905; BAE76905; BAE76905.
GeneID; 947315; -.
KEGG; ecj:JW2804; -.
KEGG; eco:b2836; -.
PATRIC; fig|1411691.4.peg.3898; -.
EchoBASE; EB1630; -.
EcoGene; EG11679; aas.
eggNOG; ENOG4105CEY; Bacteria.
eggNOG; COG0204; LUCA.
eggNOG; COG0318; LUCA.
HOGENOM; HOG000004907; -.
InParanoid; P31119; -.
KO; K05939; -.
PhylomeDB; P31119; -.
BioCyc; EcoCyc:AAS-MONOMER; -.
BioCyc; MetaCyc:AAS-MONOMER; -.
BRENDA; 2.3.1.40; 2026.
PRO; PR:P31119; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IDA:EcoliWiki.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IDA:EcoliWiki.
GO; GO:0006631; P:fatty acid metabolic process; IGI:EcoliWiki.
GO; GO:0008654; P:phospholipid biosynthetic process; IGI:EcoliWiki.
HAMAP; MF_01162; Aas; 1.
InterPro; IPR023775; Aas.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR002123; Plipid/glycerol_acylTrfase.
Pfam; PF01553; Acyltransferase; 1.
Pfam; PF00501; AMP-binding; 1.
SMART; SM00563; PlsC; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane;
Complete proteome; Ligase; Membrane; Multifunctional enzyme;
Nucleotide-binding; Reference proteome; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 719 Bifunctional protein Aas.
/FTId=PRO_0000193046.
TRANSMEM 258 277 Helical. {ECO:0000255|HAMAP-
Rule:MF_01162}.
TRANSMEM 409 433 Helical. {ECO:0000255|HAMAP-
Rule:MF_01162}.
REGION 15 138 Acyltransferase.
REGION 233 646 AMP-binding.
ACT_SITE 36 36
MUTAGEN 36 36 H->A: Loss of 2-acyl-GPE acyltransferase
activity; retains acyl-ACP synthetase
activity. {ECO:0000269|PubMed:9515909}.
CONFLICT 15 16 RV -> AL (in Ref. 1; AAA17550).
{ECO:0000305}.
CONFLICT 202 202 P -> S (in Ref. 1; AAA17550).
{ECO:0000305}.
CONFLICT 281 281 M -> I (in Ref. 4; AAT42454).
{ECO:0000305}.
SEQUENCE 719 AA; 80700 MW; F4F1021E57835EB2 CRC64;
MLFSFFRNLC RVLYRVRVTG DTQALKGERV LITPNHVSFI DGILLGLFLP VRPVFAVYTS
ISQQWYMRWL KSFIDFVPLD PTQPMAIKHL VRLVEQGRPV VIFPEGRITT TGSLMKIYDG
AGFVAAKSGA TVIPVRIEGA ELTHFSRLKG LVKRRLFPQI TLHILPPTQV AMPDAPRARD
RRKIAGEMLH QIMMEARMAV RPRETLYESL LSAMYRFGAG KKCVEDVNFT PDSYRKLLTK
TLFVGRILEK YSVEGERIGL MLPNAGISAA VIFGAIARRR MPAMMNYTAG VKGLTSAITA
AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFA HLLMPRLAQV
KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTTNDRFM SALPLFHSFG
LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRSCTVLF GTSTFLGHYA RFANPYDFYR
LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM
DARLLSVPGI EEGGRLQLKG PNIMNGYLRV EKPGVLEVPT AENVRGEMER GWYDTGDIVR
FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA SKGEALVLFT
TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG KPDFVTLKSW VDEAEQHDE


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