ID A0A1Z4RJE9_9CYAN Unreviewed; 339 AA.
AC A0A1Z4RJE9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=NIES4101_85610 {ECO:0000313|EMBL:BAZ42592.1};
OS Calothrix sp. NIES-4101.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ42592.1, ECO:0000313|Proteomes:UP000290974};
RN [1] {ECO:0000313|EMBL:BAZ42592.1, ECO:0000313|Proteomes:UP000290974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ42592.1,
RC ECO:0000313|Proteomes:UP000290974};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; AP018280; BAZ42592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RJE9; -.
DR Proteomes; UP000290974; 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:UP000290974}.
FT DOMAIN 144..257
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 339 AA; 37856 MW; BB1E6E822AC62D4E CRC64;
MFGLIGHLTS LEHAQSVARE LGYPEYADQD LDFWCSAPPQ IVDNITVTSV TGQKIEGQYV
ESCFLPEMLA TRRIKAATRK ILNAMAHAQK HDIHITALGG FSSIIFENFN LEQFRQVRNT
TLEFERFTTG NTHTAYIISK QVEEASKQVG INLSEATVAV CGATGDIGSA VCRWLDAKTD
VKELLLIARN QERLQDLQTE LGRGKIMALE QALPEADIIV WVASMPKGVE INPAILKKPC
LIIDGGYPKN LATKVQHPDI CVLNGGIVEH SLDIDWKIMQ IVNMDVPARQ LFACFAESML
LEFEKLRTNF SWGRNQITVE KMSYIGQISL KHGFRPLLV
//
