ID U5DEC6_9CHRO Unreviewed; 347 AA.
AC U5DEC6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=KR51_00035760 {ECO:0000313|EMBL:ERN39976.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN39976.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN39976.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN39976.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERN39976.1}.
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DR EMBL; ASSJ01000083; ERN39976.1; -; Genomic_DNA.
DR RefSeq; WP_022609200.1; NZ_ASSJ01000083.1.
DR AlphaFoldDB; U5DEC6; -.
DR STRING; 582515.KR51_00035760; -.
DR PATRIC; fig|582515.4.peg.4018; -.
DR eggNOG; COG5322; Bacteria.
DR InParanoid; U5DEC6; -.
DR OrthoDB; 417724at2; -.
DR Proteomes; UP000016960; Unassembled WGS sequence.
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 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 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:UP000016960}.
SQ SEQUENCE 347 AA; 38112 MW; 3F96A287CD96013B CRC64;
MFGLIGHLTN LEHAQSIARH YGYEDYAGQG LDFWCAAPPQ VVDEITVTSA TGQTIQGLYV
ESCFLPEMLT NRRIKSAIRK ILNAMACAQK RGIDITALGG FSSIVFENFN LKDKMQVRDV
ALDYSRFTTG NTHTAYISCR QVEQAAARIG IDLNSATVAV CGATGDIGSA VCRWLNAKTN
VAELLLVARN QERLQALQGE LGRGKILPLE SALPLADIVV WVASMPKGVT ISPERLRKPC
LLIDGGYPKN LSTLVQSPGV FVLKGGIVEH ALDIDWQIMH LIEMDVPSRQ LFACFAEAML
LEFEQWHTNF SWGRNQITVE KMEQIGAASL KHGFQPLLNC ESVAMSA
//
