AAR_SYNE7
ID AAR_SYNE7 Reviewed; 341 AA.
AC Q54765;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Long-chain acyl-[acyl-carrier-protein] reductase;
DE Short=AAR;
DE Short=Acyl-ACP reductase;
DE EC=1.2.1.80;
GN OrderedLocusNames=Synpcc7942_1594; ORFNames=SEC0028;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RA Phung L.T., Haselkorn R.;
RT "Genes encoding the alpha subunit of carboxyltransferase of the acetyl-CoA
RT carboxylase complex and GTP cyclohydrolase I from cyanobacterium
RT Synechococcus sp. PCC 7942.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., Gonzalez A.,
RA Salinas I., McMurtry S., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC7942 cosmid 6C3.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20671186; DOI=10.1126/science.1187936;
RA Schirmer A., Rude M.A., Li X., Popova E., del Cardayre S.B.;
RT "Microbial biosynthesis of alkanes.";
RL Science 329:559-562(2010).
CC -!- FUNCTION: Catalyzes the NADP-dependent reduction of long-chain acyl-ACP
CC to the corresponding fatty aldehyde. Involved in the biosynthesis of
CC alkanes, mainly heptadecane and pentadecane, by producing the fatty
CC aldehydes used by aldehyde decarbonylase.
CC {ECO:0000269|PubMed:20671186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + holo-[ACP] + NADP(+) = a long-
CC chain fatty acyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:54176,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17176, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:133243; EC=1.2.1.80;
CC Evidence={ECO:0000269|PubMed:20671186};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + holo-[ACP] + NAD(+) = a long-
CC chain fatty acyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:54180,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17176, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:133243; EC=1.2.1.80;
CC Evidence={ECO:0000269|PubMed:20671186};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:20671186};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.9 uM for oleoyl-ACP {ECO:0000269|PubMed:20671186};
CC KM=126 uM for oleoyl-CoA {ECO:0000269|PubMed:20671186};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U59236; AAB82039.1; -; Genomic_DNA.
DR EMBL; AY120852; AAM82647.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57624.1; -; Genomic_DNA.
DR RefSeq; WP_011242364.1; NC_007604.1.
DR PDB; 6JZQ; X-ray; 2.80 A; A/B/C/D/E=1-341.
DR PDB; 6JZU; X-ray; 2.18 A; A=1-341.
DR PDB; 6JZY; X-ray; 2.10 A; A=1-341.
DR PDB; 6JZZ; X-ray; 3.01 A; A=1-341.
DR PDBsum; 6JZQ; -.
DR PDBsum; 6JZU; -.
DR PDBsum; 6JZY; -.
DR PDBsum; 6JZZ; -.
DR AlphaFoldDB; Q54765; -.
DR SMR; Q54765; -.
DR STRING; 1140.Synpcc7942_1594; -.
DR PRIDE; Q54765; -.
DR EnsemblBacteria; ABB57624; ABB57624; Synpcc7942_1594.
DR KEGG; syf:Synpcc7942_1594; -.
DR eggNOG; COG5322; Bacteria.
DR HOGENOM; CLU_801341_0_0_3; -.
DR OMA; SWGRNNI; -.
DR OrthoDB; 586944at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_1594-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_1594-MON; -.
DR SABIO-RK; Q54765; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR016836; AAR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PIRSF; PIRSF026396; UCP026396_short-chain_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR04058; AcACP_reductase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase.
FT CHAIN 1..341
FT /note="Long-chain acyl-[acyl-carrier-protein] reductase"
FT /id="PRO_0000418900"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6JZY"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6JZZ"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 74..90
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:6JZY"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6JZQ"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:6JZQ"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:6JZY"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6JZY"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:6JZY"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6JZY"
SQ SEQUENCE 341 AA; 37479 MW; 27C025F90B1DCF3B CRC64;
MFGLIGHLTS LEQARDVSRR MGYDEYADQG LEFWSSAPPQ IVDEITVTSA TGKVIHGRYI
ESCFLPEMLA ARRFKTATRK VLNAMSHAQK HGIDISALGG FTSIIFENFD LASLRQVRDT
TLEFERFTTG NTHTAYVICR QVEAAAKTLG IDITQATVAV VGATGDIGSA VCRWLDLKLG
VGDLILTARN QERLDNLQAE LGRGKILPLE AALPEADFIV WVASMPQGVV IDPATLKQPC
VLIDGGYPKN LGSKVQGEGI YVLNGGVVEH CFDIDWQIMS AAEMARPERQ MFACFAEAML
LEFEGWHTNF SWGRNQITIE KMEAIGEASV RHGFQPLALA I
