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Database: UniProt/TrEMBL
Entry: K9WD37_9CYAN
LinkDB: K9WD37_9CYAN
Original site: K9WD37_9CYAN 
ID   K9WD37_9CYAN            Unreviewed;       457 AA.
AC   K9WD37;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=Mic7113_1572 {ECO:0000313|EMBL:AFZ17447.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ17447.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ17447.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ17447.1,
RC   ECO:0000313|Proteomes:UP000010471};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003630; AFZ17447.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9WD37; -.
DR   STRING; 1173027.Mic7113_1572; -.
DR   KEGG; mic:Mic7113_1572; -.
DR   PATRIC; fig|1173027.3.peg.1745; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_3_1_3; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000010471; Chromosome.
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   CDD; cd07136; ALDH_YwdH-P39616; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010471}.
FT   DOMAIN          6..429
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        211
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   457 AA;  50616 MW;  871C151545AD3C57 CRC64;
     MLTQVPVKDI IRQQREFFAT GKTKDVAWRI EQLKRLKQAV IDYQEAIVKA VKADLGRPDF
     EAYFEITTIA EINYAIKHVK SWAKPKKVST GIEQFPASAQ VYPEPLGVVL IISPWNYPFQ
     LMISPLTGAI AAGNCAVLKP SEMAANTSKV IADLIQNTFD PAYIAVVEGG VETSQQLLEE
     KFDHIFFTGG TAIGKIVMQA AAKHLTPVTL ELGGKSPCIV DADVDLKHAA KRITWGKYLN
     AGQTCIAPDY LLVDRRIKSD LLTEIQKCAA EFYGDDPSQS PDYGRLISHR HFERLAPLLK
     DGEIVMGGQT KPEEKYIAPT LIDGVSWDSP VMQEEIFGPI LPVIEYTDLK EAIAQINAQP
     KPLALYIFSK DKQKQQQVLQ ETSSGGVCIN DTVMHVGIST LPFGGVGDSG IGSYHGKASF
     DTFSHYKSVL KKGLWFDQNW RYPPYKGKLS LLKRIIG
//
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