ID I0GYV8_ACTM4 Unreviewed; 866 AA.
AC I0GYV8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN OrderedLocusNames=AMIS_7250 {ECO:0000313|EMBL:BAL85945.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL85945.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL85945.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-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; AP012319; BAL85945.1; -; Genomic_DNA.
DR RefSeq; WP_014440842.1; NC_017093.1.
DR AlphaFoldDB; I0GYV8; -.
DR STRING; 512565.AMIS_7250; -.
DR KEGG; ams:AMIS_7250; -.
DR PATRIC; fig|512565.3.peg.729; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_0_11; -.
DR Proteomes; UP000007882; 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:UP000007882}.
FT DOMAIN 5..267
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 461..853
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 866 AA; 93472 MW; FFDF1C7DBECED7FB CRC64;
MGEREAMIDL LVRDAEKALA DYADFTQEQV DHIVGKASVA ALDKHGDLAA LAVEETGRGV
FEDKAVKNIF ACEHVTNSMA GMKTVGVIHR DDVDGITEIA DPVGVVCAVT PVTNPTSTTI
FKALLALKTR NPIVFAFHPS AQRCSAEAAR VVRDAAVAAG APAHCIQWVE QPSIQATAAL
MNHPGVATIL ATGGNGMVRA AYSTGKPALG VGAGNVPAYV HPTADVVRAV HDIVLSKTFD
NGMICASEQA VILDRGIAEQ ALREFKRLHA YVVSADEKTL LQNYIFPPDG EGTDCVGEKL
NAAVVGQSPV WIAEQAGFTV PADTSILLAE IGEVGPGEPL SREKLCPVLA MLTADDEEQG
IRYAEQMVEF HGLGHSAVVH GRDAALAERF GKRMKAVRII WNAPASQGGI GDIYNGFRPS
LTLGCGSYGH TSVSDNVSAL NLLNIKRIGR RTNNMQWFKV PAKMYFEPHA IRYFRDMPEV
ARVTIVTDHT MTKLGYVDRI SAVLRERPEP VTIQVIDSVE PEPSIDTVQR GAALMRSFRP
DTIIALGGGS PMDAAKVMWL LYEHPDIDFG DMKEKFFDVR KRAFKFPALG ALAKLVCVPT
TSGTGAEVTP FAVITDTETG QKYPLADYAL TPSVAIIDPH LTMDLPPVVT ADSGFDALTH
ATEAYVSVYA SDFTDGLALH AIKLIFGNLE QAVRHGDTDP VAREKMHNAG TIAGMSFGNA
FLGIVHAMAH TLGATFHVAH GRTNAILLPH VIRHNGTVPS KLNSWPKYER YVAPERFQDI
ARHLGLPADT PEQGVESYAR AVERLRDAVG IPPSFQGAGV NEQEFLAALP QQAMNAYLDQ
CAPANPRMPM LEDLRRIMED AYYGTK
//
