ID   AAR_SYNY3               Reviewed;         340 AA.
AC   Q55687;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 127.
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=sll0209;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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   -!- 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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- DISRUPTION PHENOTYPE: Abolishes the presence of alkanes.
CC       {ECO:0000269|PubMed:20671186}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA10216.1; -; Genomic_DNA.
DR   PIR; S76364; S76364.
DR   AlphaFoldDB; Q55687; -.
DR   SMR; Q55687; -.
DR   IntAct; Q55687; 1.
DR   STRING; 1148.1001588; -.
DR   PaxDb; Q55687; -.
DR   EnsemblBacteria; BAA10216; BAA10216; BAA10216.
DR   KEGG; syn:sll0209; -.
DR   eggNOG; COG5322; Bacteria.
DR   InParanoid; Q55687; -.
DR   OMA; SWGRNNI; -.
DR   PhylomeDB; Q55687; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016836; AAR.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   PIRSF; PIRSF026396; UCP026396_short-chain_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR04058; AcACP_reductase; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..340
FT                   /note="Long-chain acyl-[acyl-carrier-protein] reductase"
FT                   /id="PRO_0000418901"
SQ   SEQUENCE   340 AA;  37651 MW;  8468F04DAAF0D4B9 CRC64;
     MFGLIGHLTS LEHAQAVAED LGYPEYANQG LDFWCSAPPQ VVDNFQVKSV TGQVIEGKYV
     ESCFLPEMLT QRRIKAAIRK ILNAMALAQK VGLDITALGG FSSIVFEEFN LKQNNQVRNV
     ELDFQRFTTG NTHTAYVICR QVESGAKQLG IDLSQATVAV CGATGDIGSA VCRWLDSKHQ
     VKELLLIARN RQRLENLQEE LGRGKIMDLE TALPQADIIV WVASMPKGVE IAGEMLKKPC
     LIVDGGYPKN LDTRVKADGV HILKGGIVEH SLDITWEIMK IVEMDIPSRQ MFACFAEAIL
     LEFEGWRTNF SWGRNQISVN KMEAIGEASV KHGFCPLVAL