GenomeNet

Database: UniProt
Entry: K8GD49_9CYAN
LinkDB: K8GD49_9CYAN
Original site: K8GD49_9CYAN 
ID   K8GD49_9CYAN            Unreviewed;       901 AA.
AC   K8GD49;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=OsccyDRAFT_4682 {ECO:0000313|EMBL:EKQ66873.1};
OS   Leptolyngbyaceae cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ66873.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ66873.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ66873.1,
RC   ECO:0000313|Proteomes:UP000001332};
RG   DOE Joint Genome Institute;
RA   Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT   "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL   Submitted (OCT-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}.
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:EKQ66873.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJUB01000019; EKQ66873.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8GD49; -.
DR   STRING; 864702.OsccyDRAFT_4682; -.
DR   PATRIC; fig|864702.5.peg.5027; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_1_1_3; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000001332; 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:UP000001332}.
FT   DOMAIN          7..416
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          474..867
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   901 AA;  98626 MW;  B661FAC514C83B9A CRC64;
     MSITNCQELE TLIQQVKAAQ EQYATYSQTQ VDRIFKQAAL AANAVRIPLA KLAVEETGMG
     VLEDKVIKNH FASEYIYNKY KHEKTCGVIE EDRSFGIQKI AEPVGVIAGI VPVTNPTSTT
     LFKALIALKT RNAIIFSPHP RAKRSTAEAA KVVLNAAIAA GAPEHLIGWI DEPTVELSQA
     LMRHPDIKLI LATGGPGMVK AAYSSGHPSL GVGAGNTPAV IDATADIQTA VSSILLSKTF
     DNGMICASEQ SVIVVDSVYQ QVKQEFIDRG AYFLSPAEKE QVGNVLLKDG HLNPAIVGQS
     VGTIAQLAGI GLVCLEDQGR HREKIENPLP CTLPKVLIAE VTDIGVSEPF SYEKLSPVLA
     MYRASDFYDA VHKAEQLVEF GGQGHTSVLY INPAHLDDIA YFKNSVKTAR VLINTPSSQG
     AIGDLYNFKL DPSLTLGCGT WGGNTLSENV TPHHLLNIKT VSERRENMLW FRVPPKIYFK
     YGCLPIALRE LAGKQRAFIV TDKPLFDLGL VSRLTTVLDE IGVNYDVFHD VEPDPTLSNV
     NKGLELLRSY QPDVIIAIGG GSPMDAAKVM WLMYEHPEVE FEGLATRFMD IRKRVYELPS
     LGQKAIMVAI PTTSGTGSEV TPFAVVTDDH AGIKYPLADY ALTPNMAIVD PELVLNMPKR
     LTAYGGIDAL THALESYVSV LTTEFTEGLA LEAIALLFKY LPRAYQNGAK DPEAREKVHY
     AATIAGMAFA NAFLGVCHSM AHKLGSTFHV PHGLANALMI SHVIRYNATD VPFKQAIFPQ
     YKYPHAKERY AKIADHLQLG GDTPDEKVER LVDAIEHLKL QLEIPRTIKE TLSEDEQAFY
     SKVEEMAEQA FDDQCTGANP RYPLIQDLKE LYTLAYLGCR IEASPYNVPE EVPALVSSGS
     H
//
DBGET integrated database retrieval system