ID   HETN_NOSS1              Reviewed;         287 AA.
AC   P37694;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Ketoacyl reductase HetN;
DE            EC=1.3.1.-;
GN   Name=hetN; OrderedLocusNames=alr5358;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8157596; DOI=10.1128/jb.176.8.2282-2292.1994;
RA   Black T.A., Wolk C.P.;
RT   "Analysis of a Het- mutation in Anabaena sp. strain PCC 7120 implicates a
RT   secondary metabolite in the regulation of heterocyst spacing.";
RL   J. Bacteriol. 176:2282-2292(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: May be involved in repressing heterocyst differentiation and
CC       may be essential for preventing all vegetative cells from
CC       differentiating.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; L22883; AAA22002.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77057.1; -; Genomic_DNA.
DR   PIR; AF2475; AF2475.
DR   PIR; C55210; C55210.
DR   RefSeq; WP_010999482.1; NZ_RSCN01000005.1.
DR   AlphaFoldDB; P37694; -.
DR   SMR; P37694; -.
DR   STRING; 103690.17134497; -.
DR   EnsemblBacteria; BAB77057; BAB77057; BAB77057.
DR   KEGG; ana:alr5358; -.
DR   eggNOG; COG0300; Bacteria.
DR   OMA; VNQNPIT; -.
DR   OrthoDB; 1261526at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043158; P:heterocyst differentiation; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Heterocyst; Oxidoreductase; Reference proteome.
FT   CHAIN           1..287
FT                   /note="Ketoacyl reductase HetN"
FT                   /id="PRO_0000054710"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        119
FT                   /note="M -> I (in Ref. 1; AAA22002)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  30391 MW;  21375C23A33574FD CRC64;
     MTTLTGKTVL LTGASRGLGV YIARALAKEQ ATVVCVSRSQ SGLAQTCNAV KAAGGKAIAI
     PFDVRNTSQL SALVQQAQDI VGPIDVLINN AGIEINGTFA NYSLAEIQSI FNTNLLAAME
     LTRLLLPSMM ERGSGRIVNI ASLAGKKGVA FNSVYSASKA GLIMWTDAMR QELVGTGVNI
     SVVCPGYVSQ TGMTVDTRVS APKLAGISTP KSVANAVVKA IKNKTTEVIV NQNPITESLT
     KLMLAVGQIS PTSVDRIYRW FGVVDFNQKR AENRVKDGYV AVESHRS