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Database: UniProt
Entry: A0A0D6L220_9CYAN
LinkDB: A0A0D6L220_9CYAN
Original site: A0A0D6L220_9CYAN 
ID   A0A0D6L220_9CYAN        Unreviewed;       292 AA.
AC   A0A0D6L220;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=NAD binding domain of 6-phosphogluconate dehydrogenase {ECO:0000313|EMBL:EKF05738.1};
GN   ORFNames=FDUTEX481_00594 {ECO:0000313|EMBL:EKF05738.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF05738.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKF05738.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
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:EKF05738.1}.
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DR   EMBL; AGCR01000004; EKF05738.1; -; Genomic_DNA.
DR   RefSeq; WP_045867753.1; NZ_JH930357.1.
DR   AlphaFoldDB; A0A0D6L220; -.
DR   STRING; 1188.FDUTEX481_00594; -.
DR   PATRIC; fig|1188.3.peg.591; -.
DR   HOGENOM; CLU_035117_0_8_3; -.
DR   OrthoDB; 9786703at2; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43580:SF9; GLYOXYLATE/SUCCINIC SEMIALDEHYDE REDUCTASE 1; 1.
DR   PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032761}.
FT   DOMAIN          2..153
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          162..279
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   292 AA;  31965 MW;  A0B881E9BD973C38 CRC64;
     MKVAFLGTGL MGLPMAQRLL AANIELVAYN RTPEKLAPLQ AAGAEIATHP RYAIRAADCI
     ILMLTNAAAI YSVLLSDTSW RTLSGRTVIQ MGTITPTESQ EIRDAVVAAG GEYLEAPVLG
     SIPEAQTGKL IVMVGAREDQ FQRYLNLLQN FGPEPRLVGP VGAAASVKLA LNQLIASLTT
     SFALSLAFVQ RQGIDVEKFM EILRESVLYA PTFDKKLARM LDGNFANPNF PTKHLLKDTD
     LFINEAKTVE LDVSSIKGVR QILHSAMKMS FANDDYSAVF YAIKAWEEGR WE
//
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