AAS_ECODH
ID AAS_ECODH Reviewed; 719 AA.
AC B1XDP2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Bifunctional protein Aas {ECO:0000255|HAMAP-Rule:MF_01162};
DE Includes:
DE RecName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE EC=2.3.1.40 {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=2-acyl-GPE acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE Includes:
DE RecName: Full=Acyl-[acyl-carrier-protein] synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE EC=6.2.1.20 {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=Acyl-ACP synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase {ECO:0000255|HAMAP-Rule:MF_01162};
GN Name=aas {ECO:0000255|HAMAP-Rule:MF_01162}; OrderedLocusNames=ECDH10B_3006;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
CC -!- FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty
CC acids to the 1-position via an enzyme-bound acyl-ACP intermediate in
CC the presence of ATP and magnesium. Its physiological function is to
CC regenerate phosphatidylethanolamine from 2-acyl-glycero-3-
CC phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or
CC degradation by phospholipase A1. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP]
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP];
CC Xref=Rhea:RHEA:10304, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:64612, ChEBI:CHEBI:65213,
CC ChEBI:CHEBI:138651; EC=2.3.1.40; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01162};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01162}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01162}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC acetyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent
CC AMP-binding enzyme family. {ECO:0000255|HAMAP-Rule:MF_01162}.
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DR EMBL; CP000948; ACB03946.1; -; Genomic_DNA.
DR RefSeq; WP_000899054.1; NC_010473.1.
DR AlphaFoldDB; B1XDP2; -.
DR SMR; B1XDP2; -.
DR KEGG; ecd:ECDH10B_3006; -.
DR HOGENOM; CLU_000022_59_8_6; -.
DR OMA; ANWVYLE; -.
DR BioCyc; ECOL316385:ECDH10B_RS15280-MON; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR HAMAP; MF_01162; Aas; 1.
DR InterPro; IPR023775; Aas.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SMART; SM00563; PlsC; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane; Ligase;
KW Membrane; Multifunctional enzyme; Nucleotide-binding; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..719
FT /note="Bifunctional protein Aas"
FT /id="PRO_1000137888"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT TRANSMEM 409..433
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT REGION 15..138
FT /note="Acyltransferase"
FT REGION 233..646
FT /note="AMP-binding"
FT ACT_SITE 36
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
SQ 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
