PALAD_THUAT
ID PALAD_THUAT Reviewed; 387 AA.
AC Q41510;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Acyl-[acyl-carrier-protein] 6-desaturase {ECO:0000305};
DE EC=1.14.19.26 {ECO:0000269|PubMed:7961667, ECO:0000269|PubMed:9144157};
DE AltName: Full=Palmitoyl-acyl carrier protein desaturase {ECO:0000303|PubMed:7961667};
DE Flags: Precursor;
OS Thunbergia alata (Black-eyed Susan vine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Acanthaceae; Thunbergioideae; Thunbergia.
OX NCBI_TaxID=32198 {ECO:0000312|EMBL:AAA82160.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE
RP SPECIFICITY, AND ACTIVITY REGULATION.
RC TISSUE=Endosperm;
RX PubMed=7961667; DOI=10.1016/s0021-9258(18)47015-9;
RA Cahoon E.B., Cranmer A.M., Shanklin J., Ohlrogge J.B.;
RT "delta 6 Hexadecenoic acid is synthesized by the activity of a soluble
RT delta 6 palmitoyl-acyl carrier protein desaturase in Thunbergia alata
RT endosperm.";
RL J. Biol. Chem. 269:27519-27526(1994).
RN [2]
RP 3D-STRUCTURE MODELING, MUTAGENESIS OF ALA-207; ALA-214; TYR-215; ALA-226;
RP SER-231; LEU-232 AND GLY-233, AND CATALYTIC ACTIVITY.
RX PubMed=9144157; DOI=10.1073/pnas.94.10.4872;
RA Cahoon E.B., Lindqvist Y., Schneider G., Shanklin J.;
RT "Redesign of soluble fatty acid desaturases from plants for altered
RT substrate specificity and double bond position.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4872-4877(1997).
CC -!- FUNCTION: Delta(6) fatty acid desaturase introducing a cis double bond
CC at carbon 6 of palmitoyl-[acyl-carrier protein](16:0-ACP), producing
CC 16:1(6Z)-ACP (PubMed:7961667, PubMed:9144157). No activity with the
CC coenzyme A ester of the fatty acid (PubMed:7961667). The position of
CC the double bond is determined by its distance from the carboxyl end of
CC the fatty acid (PubMed:7961667). Low activity with several saturated
CC acyl-[acyl-carrier protein]s, including 14:0-ACP and 18:0-ACP
CC (PubMed:7961667, PubMed:9144157). Requires reduced ferredoxin for
CC detectable in vitro activity (PubMed:7961667).
CC {ECO:0000269|PubMed:7961667, ECO:0000269|PubMed:9144157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (6Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:46416, Rhea:RHEA-COMP:9652, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:11556,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78483,
CC ChEBI:CHEBI:86110; EC=1.14.19.26;
CC Evidence={ECO:0000269|PubMed:7961667, ECO:0000269|PubMed:9144157};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
CC -!- ACTIVITY REGULATION: Inhibited by KCN or H(2)O(2).
CC {ECO:0000269|PubMed:7961667}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; U09269; AAA82160.1; -; mRNA.
DR PDB; 7PP7; X-ray; 2.05 A; A=44-387.
DR PDBsum; 7PP7; -.
DR AlphaFoldDB; Q41510; -.
DR SMR; Q41510; -.
DR BioCyc; MetaCyc:MON-12584; -.
DR BRENDA; 1.14.19.26; 6365.
DR UniPathway; UPA00199; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01050; Acyl_ACP_Desat; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR005067; Fatty_acid_desaturase-2.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR PANTHER; PTHR31155; PTHR31155; 1.
DR Pfam; PF03405; FA_desaturase_2; 1.
DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Plastid; Transit peptide.
FT TRANSIT 1..29
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 30..387
FT /note="Acyl-[acyl-carrier-protein] 6-desaturase"
FT /id="PRO_0000434767"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 255
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 255
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT MUTAGEN 207
FT /note="A->T: Catalytic activity converted to a delta(9)-
FT 18:0-ACP desaturase; when associated with F-226; N-231; T-
FT 232 and A-233. Catalyzes both delta(9) desaturation of
FT 18:0-ACP and delta(6) desaturation of 16:0-ACP; when
FT associated with F-226. Gain of a delta(9) desaturase
FT activity with both 18:0-ACP and 16:0-ACP; when associated
FT with F-226; N-231; T-232 and A-233."
FT /evidence="ECO:0000269|PubMed:9144157"
FT MUTAGEN 214
FT /note="A->G: Broadened fatty acid chain-length specificity;
FT when associated with F-215."
FT /evidence="ECO:0000269|PubMed:9144157"
FT MUTAGEN 215
FT /note="Y->F: Broadened fatty acid chain-length specificity;
FT when associated with G-214."
FT /evidence="ECO:0000269|PubMed:9144157"
FT MUTAGEN 226
FT /note="A->F: Catalytic activity converted to a delta(9)-
FT 18:0-ACP desaturase; when associated with T-207; N-231; T-
FT 232 and A-233. Catalyzes both delta(9) desaturation of
FT 18:0-ACP and delta(6) desaturation of 16:0-ACP; when
FT associated with T-207. Gain of a delta(9) desaturase
FT activity with both 18:0-ACP and 16:0-ACP; when associated
FT with T-207; N-231; T-232 and A-233."
FT /evidence="ECO:0000269|PubMed:9144157"
FT MUTAGEN 231
FT /note="S->N: Catalytic activity converted to a delta(9)-
FT 18:0-ACP desaturase; when associated with T-207; F-226; T-
FT 232 and A-233. Gain of a delta(9) desaturase activity with
FT both 18:0-ACP and 16:0-ACP; when associated with T-207; F-
FT 226; T-232 and A-233."
FT /evidence="ECO:0000269|PubMed:9144157"
FT MUTAGEN 232
FT /note="L->T: Catalytic activity converted to a delta(9)-
FT 18:0-ACP desaturase; when associated with T-207; F-226; N-
FT 231 and A-233. Gain of a delta(9) desaturase activity with
FT both 18:0-ACP and 16:0-ACP; when associated with T-207; F-
FT 226; N-231 and A-233."
FT /evidence="ECO:0000269|PubMed:9144157"
FT MUTAGEN 233
FT /note="G->A: Catalytic activity converted to a delta(9)-
FT 18:0-ACP desaturase; when associated with T-207; F-226; N-
FT 231 and T-232. Gain of a delta(9) desaturase activity with
FT both 18:0-ACP and 16:0-ACP; when associated with T-207; F-
FT 226; N-231 and T-232."
FT /evidence="ECO:0000269|PubMed:9144157"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:7PP7"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:7PP7"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 157..183
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 211..238
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 242..272
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:7PP7"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:7PP7"
SQ SEQUENCE 387 AA; 43868 MW; B29E03180FB7EC68 CRC64;
MALVFKSIGA HKTPPCTLNL ASPALYHTRV TMASTITHPP PLKDRKISST RRVRTYPLAP
EKAEIFNSMH GWVEDTILPF LKPVEESWQP TDFLPDSTSD GFHEQVEELR KRTADLPDDY
LVALVGAMVT EEALPTYQTM LNTTDVIYDE SGASPVPWAV WTRAWTAEEN RHGDIVNKYL
YLSGRVDMKQ IEKTIQYLIG SGMDPGADNN PYLAYIYTSY QERATAISHG SLGRLARQKG
EMKLAQICGT ISADEKRHEA AYSKIVEKLF ELDPEGTMLA LAYMMKMKIV MPARLMHDGK
DPDMFQHFSA VSQRLGIYTA KEYTDILEHM IARWGVDKLT GLSGEGRRAQ DYVCGLPMRF
RKVEERAQAW AENISHVPFS WIFGRRV
