ID A0A090J2R1_9BACI Unreviewed; 383 AA.
AC A0A090J2R1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=L-threonine dehydrogenase {ECO:0000313|EMBL:AWI12974.1};
DE SubName: Full=Putative alcohol dehydrogenase {ECO:0000313|EMBL:CEE02160.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:CEE02160.1};
GN Name=yiaY {ECO:0000313|EMBL:CEE02160.1};
GN ORFNames=BT1A1_2339 {ECO:0000313|EMBL:CEE02160.1}, CQJ30_12900
GN {ECO:0000313|EMBL:AWI12974.1};
OS Caldibacillus thermoamylovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE02160.1, ECO:0000313|Proteomes:UP000040576};
RN [1] {ECO:0000313|EMBL:CEE02160.1, ECO:0000313|Proteomes:UP000040576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg Daniel;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AWI12974.1, ECO:0000313|Proteomes:UP000244914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSBM {ECO:0000313|EMBL:AWI12974.1,
RC ECO:0000313|Proteomes:UP000244914};
RX PubMed=29625286; DOI=10.1016/j.biortech.2018.03.121;
RA Cai L., Zheng S.W., Shen Y.J., Zheng G.D., Liu H.T., Wu Z.Y.;
RT "Complete genome sequence provides insights into the biodrying-related
RT microbial function of Bacillus thermoamylovorans isolated from sewage
RT sludge biodrying material.";
RL Bioresour. Technol. 260:141-149(2018).
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; CP023704; AWI12974.1; -; Genomic_DNA.
DR EMBL; CCRF01000065; CEE02160.1; -; Genomic_DNA.
DR RefSeq; WP_034771364.1; NZ_JAQEZG010000008.1.
DR AlphaFoldDB; A0A090J2R1; -.
DR KEGG; bthv:CQJ30_12900; -.
DR Proteomes; UP000040576; Unassembled WGS sequence.
DR Proteomes; UP000244914; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08188; PDDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CEE02160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000040576}.
FT DOMAIN 9..375
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 383 AA; 40982 MW; 089273CBA276BCBF CRC64;
MATSEFYMPT VNLFGVNKVQ EVGSRLKGLG CKKTLIVTDE GIKSLGYADQ VAGIVREAGL
EVVIYSEVKP NPTDKNVEAG LKIFTEENCD SIISLGGGSP HDCAKGIGLV AANGGTIHDY
EGVDRSAKPM VPLAAINTTA GTASEMTKFT IITDTSRKVK MAIVDKHVTP TFSVNDPMLM
IGMPPSLTAA TGLDALTHAV EAYVSTAATP ITDACALKAI EIIPEFLPRA FANGQDLEAR
EQMIYAQYLA GMAFNNASLG YVHAIAHQFG GFYDLPHGVC NAILLPHVSR FNLVARPDRF
RNIAIALGEN VKGLSTYEAA EKAIATIERL ARDMNIPNGF KELGAKEEDI PVLAEHAMAD
ACAATNPRKA KLEEVMEIIR QAM
//
