ID Q55811_SYNY3 Unreviewed; 456 AA.
AC Q55811;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN OrderedLocusNames=slr0091 {ECO:0000313|EMBL:BAA10564.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC Synechocystis.
OX NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA10564.1, ECO:0000313|Proteomes:UP000001425};
RN [1] {ECO:0000313|EMBL:BAA10564.1, ECO:0000313|Proteomes:UP000001425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; BA000022; BAA10564.1; -; Genomic_DNA.
DR PIR; S76620; S76620.
DR AlphaFoldDB; Q55811; -.
DR SMR; Q55811; -.
DR IntAct; Q55811; 3.
DR STRING; 1148.gene:10500068; -.
DR PaxDb; 1148-1001727; -.
DR EnsemblBacteria; BAA10564; BAA10564; BAA10564.
DR KEGG; syn:slr0091; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; Q55811; -.
DR PhylomeDB; Q55811; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR CDD; cd07087; ALDH_F3-13-14_CALDH-like; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
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; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000001425}.
FT DOMAIN 5..428
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT COILED 23..50
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 210
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 244
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 456 AA; 51188 MW; 579562C73A14786D CRC64;
MNTAKTVVAE QRDFFRQGKT KSVQDRLTAL AKLKTQIQAQ EEEIIKALKQ DFGKPTFESY
VNEILGVIRE INYYQKHLQQ WSKPQRVGTN LMVFPASAQL RPEPLGVVLI ISPWNYPFYL
CLMPLIGAIA AGNCVVVKPS EYTPAISGVI TRLIQNVFSP AWATVVEGDE TISQQLLQEK
FDHIFFTGSP RVGRLIMAAA AEQLTPVTLE LGGKSPCVVD REINLQETAK RIMWGKLVNA
GQTCVAPDYL LVEQSCLEQL LPALQQAIQM LFGENPAHSP DYTRIVNQQQ WSRLVSLLSH
GKVITRGDHN EGDRYIAPTL IIDPDLNSPL MQEEIFGPIL PILTYQSLSE AIDFINIKPK
PLALYFFSNN RQKQEEILQS TSSGSVCLND ILLHLTVTDL PFGGVGESGM GRYHGKATFD
TLSNYKSILR RPFWGETNLR YSPYGKKMNL IKKLFS
//