ACP1_SPIOL
ID ACP1_SPIOL Reviewed; 138 AA.
AC P07854;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Acyl carrier protein 1, chloroplastic;
DE Short=ACP I;
DE Short=Acyl carrier protein I;
DE Flags: Precursor;
GN Name=ACL1.1;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX AGRICOLA=IND92000043; DOI=10.1007/BF00015645;
RA Scherer D.E., Knauf V.C.;
RT "Isolation of a cDNA clone for the acyl carrier protein-I of spinach.";
RL Plant Mol. Biol. 9:127-134(1987).
RN [2]
RP PROTEIN SEQUENCE OF 57-138.
RC TISSUE=Leaf;
RX PubMed=6486822; DOI=10.1016/0003-9861(84)90351-5;
RA Kuo T.M., Ohlrogge J.B.;
RT "The primary structure of spinach acyl carrier protein.";
RL Arch. Biochem. Biophys. 234:290-296(1984).
RN [3]
RP STRUCTURE BY NMR OF 57-138 IN COMPLEX WITH PHOSPHOPANTETHEINE, AND
RP PHOSPHOPANTETHEINYLATION AT SER-94.
RX PubMed=16618110; DOI=10.1021/bi052062d;
RA Zornetzer G.A., Fox B.G., Markley J.L.;
RT "Solution structures of spinach acyl carrier protein with decanoate and
RT stearate.";
RL Biochemistry 45:5217-5227(2006).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- INTERACTION:
CC P07854; P22337; Xeno; NbExp=2; IntAct=EBI-15944962, EBI-15944981;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-ACP by acpS. This modification is essential for activity because
CC fatty acids are bound in thioester linkage to the sulfhydryl of the
CC prosthetic group (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; M17636; AAA34023.1; -; mRNA.
DR PIR; A28052; AYSP.
DR PDB; 2AVA; NMR; -; A=57-138.
DR PDB; 2FVA; NMR; -; A=57-138.
DR PDB; 2FVE; NMR; -; A=57-138.
DR PDB; 2FVF; NMR; -; A=57-138.
DR PDB; 2XZ0; X-ray; 3.00 A; D=57-138.
DR PDB; 2XZ1; X-ray; 3.35 A; C/D=57-138.
DR PDBsum; 2AVA; -.
DR PDBsum; 2FVA; -.
DR PDBsum; 2FVE; -.
DR PDBsum; 2FVF; -.
DR PDBsum; 2XZ0; -.
DR PDBsum; 2XZ1; -.
DR AlphaFoldDB; P07854; -.
DR BMRB; P07854; -.
DR SMR; P07854; -.
DR DIP; DIP-60378N; -.
DR IntAct; P07854; 1.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P07854; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR044813; ACP_chloroplastic.
DR InterPro; IPR003231; Acyl_carrier.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR46153; PTHR46153; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR00517; acyl_carrier; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Phosphopantetheine; Phosphoprotein; Plastid;
KW Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:6486822"
FT CHAIN 57..138
FT /note="Acyl carrier protein 1, chloroplastic"
FT /id="PRO_0000000584"
FT DOMAIN 59..134
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 94
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:16618110"
FT CONFLICT 66
FT /note="C -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2XZ0"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:2XZ0"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2XZ0"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2XZ0"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2FVA"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2XZ0"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:2XZ0"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2XZ0"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:2XZ0"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2XZ0"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:2XZ0"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2XZ0"
SQ SEQUENCE 138 AA; 14909 MW; B3FB8F08BF657980 CRC64;
MASLSATTTV RVQPSSSSLH KLSQGNGRCS SIVCLDWGKS SFPTLRTSRR RSFISAAKKE
TIDKVCDIVK EKLALGADVV VTADSEFSKL GADSLDTVEI VMNLEEEFGI NVDEDKAQDI
STIQQAADVI ESLLEKKA
