ID A0A060QEZ7_9PROT Unreviewed; 349 AA.
AC A0A060QEZ7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Dehydrogenases with different specificities (Related to short-chain alcohol dehydrogenases) {ECO:0000313|EMBL:CDG39510.1};
GN ORFNames=ASAP_1465 {ECO:0000313|EMBL:CDG39510.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG39510.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG39510.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39510.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24682158; DOI=10.1093/gbe/evu062;
RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT life in insect guts.";
RL Genome Biol. Evol. 6:912-920(2014).
RN [2] {ECO:0000313|EMBL:CDG39510.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39510.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA Lievens P.M., Daffonchio D., Bandi C.;
RT "Evolution of mitochondria reconstructed from the energy metabolism of
RT living bacteria.";
RL PLoS ONE 9:e96566-e96566(2014).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:CDG39510.1}.
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DR EMBL; CBLX010000009; CDG39510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060QEZ7; -.
DR eggNOG; COG1028; Bacteria.
DR Proteomes; UP000027583; Unassembled WGS sequence.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR48107; NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR48107:SF33; SHORT CHAIN DEHYDROGENASE; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 36703 MW; 1838AE23E896FAC0 CRC64;
MTDPTDKKTI KTTTPGGASP ATNRRSMMQG ATLGLAGLVA GSSRAQAAPD ATAVSAPLAD
PQKLYPHAPF ASQPQEWPGL QSRMHPKPDC GETSYKGSGR MAGRRALITG GDSGLGRAIA
IAYAREGADI AINYLPQEEE DAREVVALIR KAGRKAIALP GDIRDEAFCQ KLVSDAASQL
GGLDTLVNCA GRQHYHESIL ELSTEEFDWT LKTNLYALFW IIKAAIPHMP PGSAIVNTAS
SNAYNPSEII IDYSLTKAGI ANLTKSLAKQ LLPKGIRINA VAPGPFWTPL QVCGGQPMSA
VEKYGTTVPM GRPGQPAEIA PVYVTLASTE GSYITGQIYG ITGGTGMPG
//
