(data stored in ACNUC7421 zone)

SWISSPROT: D1CDG9_THET1

ID   D1CDG9_THET1            Unreviewed;       338 AA.
AC   D1CDG9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962511};
DE            EC=2.3.1.274 {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS01132328};
DE   AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000256|HAMAP-Rule:MF_00019};
DE   AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_00019};
DE   AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000256|HAMAP-Rule:MF_00019};
GN   Name=plsX {ECO:0000256|HAMAP-Rule:MF_00019};
GN   OrderedLocusNames=Tter_0052 {ECO:0000313|EMBL:ACZ40975.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40975.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40975.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate
CC       (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This
CC       enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC       {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962504}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate +
CC         holo-[ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685,
CC         Rhea:RHEA-COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:138651; EC=2.3.1.274;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00019,
CC         ECO:0000256|SAAS:SAAS01132329};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962503}.
CC   -!- SUBUNIT: Homodimer. Probably interacts with PlsY.
CC       {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00019}.
CC       Note=Associated with the membrane possibly through PlsY.
CC       {ECO:0000256|HAMAP-Rule:MF_00019}.
CC   -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000256|HAMAP-
CC       Rule:MF_00019, ECO:0000256|SAAS:SAAS00962509}.
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DR   EMBL; CP001825; ACZ40975.1; -; Genomic_DNA.
DR   RefSeq; WP_012874010.1; NC_013525.1.
DR   STRING; 525904.Tter_0052; -.
DR   EnsemblBacteria; ACZ40975; ACZ40975; Tter_0052.
DR   KEGG; ttr:Tter_0052; -.
DR   eggNOG; ENOG4105C6B; Bacteria.
DR   eggNOG; COG0416; LUCA.
DR   HOGENOM; HOG000154731; -.
DR   KO; K03621; -.
DR   OMA; DCKPEYL; -.
DR   OrthoDB; 631784at2; -.
DR   BioCyc; TTER525904:G1GGS-52-MONOMER; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00019; PlsX; 1.
DR   InterPro; IPR003664; FA_synthesis.
DR   InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR   PANTHER; PTHR30100; PTHR30100; 1.
DR   Pfam; PF02504; FA_synthesis; 1.
DR   PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR   TIGRFAMs; TIGR00182; plsX; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDG9.
DR   SWISS-2DPAGE; D1CDG9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962513};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962512};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962501};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962507};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962500}.
SQ   SEQUENCE   338 AA;  35930 MW;  9E85A80C5920F25D CRC64;
     MRVAVDAMGG DKAPDEIVEG ALRASNELGI DITLVGKEDV IAPLLSSKPS QRHIEIIHTP
     EIIAMDEHPA TAVRKKKDSS IVRGLELLKE GKADAFVSAG NSGAVMAASL FVLGRCTGID
     RPAIGTIIPG KEGPVLLIDA GANVDPEPVH LLQFAFMGSI YAREVMRIGN PKVGLLSNGE
     EETKGNKLTL QAHKLLKGSN LNFQGNVEGR DVTKGTVHVI VTDGFTGNVV LKTVEGVAED
     LVSIIREEIT SGILNKVGAL ILQGAFRKVA QKLDYAEYGG APLLGVRGNV FIAHGRSNAK
     AIKNAIRLAH EAASHRIPKL ISDNNIIVTG KEMFQQDL
//

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