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
//