ID K9VR00_9CYAN Unreviewed; 876 AA.
AC K9VR00;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=Osc7112_5389 {ECO:0000313|EMBL:AFZ09625.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ09625.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ09625.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ09625.1,
RC ECO:0000313|Proteomes:UP000010478};
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., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000256|ARBA:ARBA00035645,
CC ECO:0000256|PIRNR:PIRNR000111}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00035641,
CC ECO:0000256|PIRNR:PIRNR000111}.
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DR EMBL; CP003614; AFZ09625.1; -; Genomic_DNA.
DR RefSeq; WP_015178833.1; NC_019729.1.
DR AlphaFoldDB; K9VR00; -.
DR STRING; 179408.Osc7112_5389; -.
DR KEGG; oni:Osc7112_5389; -.
DR PATRIC; fig|179408.3.peg.6731; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_1_3; -.
DR OrthoDB; 9804734at2; -.
DR Proteomes; UP000010478; Chromosome.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd08178; AAD_C; 1.
DR CDD; cd07122; ALDH_F20_ACDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald-ADH.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000111};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478}.
FT DOMAIN 6..400
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 456..852
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 876 AA; 95677 MW; E25A91573376A071 CRC64;
MKVTNVDELE VLIQKVKAAQ AEFATYTQEQ VDRIFKQAAL AANAARIPLA KAAVKESGMG
VIEDKAIKNH FASEMIYNKY KNDKTCGIIE SDRHFGYERI AEPVGVLAGI VPVTNPTSTT
IFKSLIVLKT RNGIIFSPHP RAKSCTAAAA KIILDAAVAA GAPPDIIGWI DEPTVPLSQA
LMQHPDIKLI LATGGPGMVK AAYSSGHPSL GVGAGNTPAI IDETAHIQMA VSSILLSKTF
DNGTICASEQ SVVVVDEVYD AVQLEFIKRG AYFLNAEERE KVRQVILIDG RLNAELVGQS
VQKVAEVAGF EVPSNIRVLI GEVEAVGKEE PLACEKLSPI LAMYRAKDFT EAVDKAEALI
IFGGHGHTSV LYTAPHNQKH IRYFESKVET SRVLINTPSS QGAIGDLYNF RLDPSLTLGC
GSWGDNSISV NVTPHHLLNI KTVAERRENM LWFRIPPKIY FKSGCLPVAL RDLAGKKRAL
IVTDKPLFEL GLIKEVTDSL EEIGIDHYTF YDVEPDPSLA TVRKGLQICN SFHPDVIIAF
GGGSPMDAAK VMWLMYEHPE IEFEGLAMRF MDIRKRVYEL PPLGSKAIMV AIPTTSGTGS
EVTPFAVVTD EQSGIKYPLA DYALTPSMAI VDPELTLNMP RKLTAYGGID ALTHALEAYV
SVLASEYTNG LALEAIRLLF KYLPSAYKNG ASDPKAREKV HYAATIAGMA FANAFLGVCH
SIAHQLGATC HVPHGLANAL MISHVIRYNA TDVPFKQAIF SQNKYPNSKW RYARIADYLN
LGGDTEEEKV EKLIAAVEDL KRQVDIPSTI QEAIASQGMS DDFFFARVEE MADRAFDDQC
TGANPRYPLI EDLKQLLVQA YSHGDTSEVD RVLTVV
//
