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Database: UniProt
Entry: A0A0D6KE96_9CYAN
LinkDB: A0A0D6KE96_9CYAN
Original site: A0A0D6KE96_9CYAN 
ID   A0A0D6KE96_9CYAN        Unreviewed;       498 AA.
AC   A0A0D6KE96;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=FDUTEX481_04710 {ECO:0000313|EMBL:EKE97760.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE97760.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKE97760.1, 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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
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:EKE97760.1}.
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DR   EMBL; AGCR01000110; EKE97760.1; -; Genomic_DNA.
DR   RefSeq; WP_045873905.1; NZ_JH930372.1.
DR   AlphaFoldDB; A0A0D6KE96; -.
DR   STRING; 1188.FDUTEX481_04710; -.
DR   PATRIC; fig|1188.3.peg.8696; -.
DR   HOGENOM; CLU_005391_0_1_3; -.
DR   OrthoDB; 548310at2; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032761}.
FT   DOMAIN          34..493
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   498 AA;  54005 MW;  18BECB2294ECC895 CRC64;
     MTTQLTPPQS QTTIRTYQNF INGKYISPLS GVNYERKSPL TGETIVQIPW SNQADTDVAI
     QAARQVFDDG TWSTSHARVR HDILRKTAEL LTTKTSEIAA VICQEVGRPI GMCIGEVQMT
     AQVFDYFAAL TLNLQGESTT QYDRNAIGLT VHEPVGVVGI ITPWNFPLLL VAWKIAPAIA
     AGCTMVVKPS EFTPSTAFML AEILSEAGLP DGVINIVTGD GPVVGEHLVE SPLVDKIAFT
     GSTAVGRRIM AKGAPTLKRM SLELGGKSPN IVFGDADLSQ AIPGALFGIY INSGQVCQAG
     SRLLLHESIK DVFIEQFLAA TQTFQIGNPT DNTTMMGPVI NEIQFERIQN YIQLGEKEGA
     KLLIGGSGRY LVPGFEQGLF IKPTVFDHVT NEMAIAQEEI FGPVLSIMTF KDKAEALQIA
     NQTMYGLTAA IWTKNLDTAF KMAKGIRAGT VWVNSYHTSG LEPTMPYGGY KQSGIGREVG
     KNGLEEYLET KAIHIKLA
//
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