ID A3PBQ7_PROM0 Unreviewed; 346 AA.
AC A3PBQ7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Long-chain acyl-[acyl-carrier-protein] reductase {ECO:0000256|PIRNR:PIRNR026396};
DE Short=AAR {ECO:0000256|PIRNR:PIRNR026396};
DE EC=1.2.1.80 {ECO:0000256|PIRNR:PIRNR026396};
GN OrderedLocusNames=P9301_05591 {ECO:0000313|EMBL:ABO17182.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17182.1, ECO:0000313|Proteomes:UP000001430};
RN [1] {ECO:0000313|EMBL:ABO17182.1, ECO:0000313|Proteomes:UP000001430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17182.1,
RC ECO:0000313|Proteomes:UP000001430};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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:0000256|PIRNR:PIRNR026396}.
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:0000256|PIRNR:PIRNR026396};
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:0000256|PIRNR:PIRNR026396};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRNR:PIRNR026396};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|PIRNR:PIRNR026396}.
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DR EMBL; CP000576; ABO17182.1; -; Genomic_DNA.
DR RefSeq; WP_011862552.1; NC_009091.1.
DR AlphaFoldDB; A3PBQ7; -.
DR STRING; 167546.P9301_05591; -.
DR KEGG; pmg:P9301_05591; -.
DR eggNOG; COG5322; Bacteria.
DR HOGENOM; CLU_801341_0_0_3; -.
DR OrthoDB; 417724at2; -.
DR Proteomes; UP000001430; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR016836; AAR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR NCBIfam; TIGR04058; AcACP_reductase; 1.
DR PANTHER; PTHR43086:SF3; NADP-DEPENDENT 3-HYDROXY ACID DEHYDROGENASE YDFG; 1.
DR PANTHER; PTHR43086; VERY-LONG-CHAIN 3-OXOOACYL-COA REDUCTASE; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR PIRSF; PIRSF026396; UCP026396_short-chain_DH; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR026396};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR026396};
KW Reference proteome {ECO:0000313|Proteomes:UP000001430}.
FT DOMAIN 149..260
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 346 AA; 38455 MW; 4B778B77C464E226 CRC64;
MFGLIGHSTS FEDAKRKASM LGFDHIADGD LDVWCTAPPQ LVENVEVKSA TGISIEGSYI
DSCFVPEMLS RFKTARRKVL NAMELAQKKG INITALGGFT SIIFENFNLL QHKQIRNTSL
EWERFTTGNT HTAWVICKQL EINAPRIGID LKKATVAVIG ATGDIGSAVC RWLINKTGIS
ELLMVARQQE PLALLQKELD GGTITSLDEA LPQADIVVWV ASMPKTIEID TDNLKKPCLM
IDGGYPKNLD EKFQGENIYV LKGGIVEFFN DIGWNMMELA EMQNPQREMF ACFAEAMILE
FEKCHTNFSW GRNNISLEKM EFIGAASLKH GFSAIGLDKQ PKVLTV
//
