ID K9PSJ2_9CYAN Unreviewed; 339 AA.
AC K9PSJ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=Cal7507_5585 {ECO:0000313|EMBL:AFY35911.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY35911.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY35911.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY35911.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) 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; CP003943; AFY35911.1; -; Genomic_DNA.
DR RefSeq; WP_015131702.1; NC_019682.1.
DR AlphaFoldDB; K9PSJ2; -.
DR STRING; 99598.Cal7507_5585; -.
DR KEGG; calo:Cal7507_5585; -.
DR PATRIC; fig|99598.3.peg.6256; -.
DR eggNOG; COG5322; Bacteria.
DR HOGENOM; CLU_801341_0_0_3; -.
DR OrthoDB; 417724at2; -.
DR Proteomes; UP000010390; 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:UP000010390}.
FT DOMAIN 144..256
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 339 AA; 37670 MW; BEF081F0227058BA CRC64;
MFGLIGHLTS LEHAQAVAQE LGYPEYADQG LDFWCSAPPQ IVDNITVTSV TGQKIEGRYV
ESCFLPEMLA NRRIKAATRK ILNAMAHAQK HGINITALGG FSSIIFENFN LEQFSQVRNI
KLEFERFTTG NTHTAYIICR QVEQASKQLG IDLKSATVAV CGATGDIGSA VTRWLDAKTD
VKELLLIARN QERLQELQAE LGRGKIMALE EALPQADIVV WVASMPKGVE IDPSILKQPS
LLIDGGYPKN LATKIQYPGV HVLNGGIVEH SLDIDWKIMK IVNMDVPGRQ LFACFAESML
LEFEKLYTNF SWGRNQITVD KMEQIGQVSV KHGFRPLLV
//
