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}.
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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
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