ID K9ZHT6_ANACC Unreviewed; 339 AA.
AC K9ZHT6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Anacy_3390 {ECO:0000313|EMBL:AFZ58793.1};
OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ58793.1, ECO:0000313|Proteomes:UP000010474};
RN [1] {ECO:0000313|Proteomes:UP000010474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003659; AFZ58793.1; -; Genomic_DNA.
DR RefSeq; WP_015215419.1; NZ_AP018166.1.
DR AlphaFoldDB; K9ZHT6; -.
DR STRING; 272123.Anacy_3390; -.
DR KEGG; acy:Anacy_3390; -.
DR PATRIC; fig|272123.3.peg.3690; -.
DR eggNOG; COG5322; Bacteria.
DR HOGENOM; CLU_801341_0_0_3; -.
DR OrthoDB; 417724at2; -.
DR Proteomes; UP000010474; 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:UP000010474}.
FT DOMAIN 144..261
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 339 AA; 37825 MW; 555B74CD2F97A996 CRC64;
MFGLIGHLTS LEHAQSVAQE LGYPEYADQG LDFWCSAPPQ IVDHITVTSI TGQKIEGRYV
ESCFLPEMLA NRRIKAATRK ILNAMAHAQK HGIDITALGG FSSIIFENFN LEQFSQVRNV
KLEFERFTTG NTHTAYIICR QVEEASKQLG IELSKATVAV CGATGDIGSA VTRWLDKKTD
VQELLLIARN QERLQELQAE LGRGKIMGLQ EALPQADIVV WVASMPKGVE IDPTVLKQPC
LLIDGGYPKN LGTKIQHPGV YVLNGGIVEH SLDIDWKIMK IVNMDVPARQ LFACFAESML
LEFEKLYTNF SWGRNQITVD KMEQIGRVSI KHGFRPLLV
//
