ID A0A0D5A678_9NOCA Unreviewed; 388 AA.
AC A0A0D5A678;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AJW38632.1};
GN ORFNames=NY08_600 {ECO:0000313|EMBL:AJW38632.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW38632.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW38632.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW38632.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; CP010797; AJW38632.1; -; Genomic_DNA.
DR RefSeq; WP_045194818.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5A678; -.
DR STRING; 1564114.NY08_600; -.
DR KEGG; rhb:NY08_600; -.
DR PATRIC; fig|1564114.4.peg.593; -.
DR HOGENOM; CLU_007207_0_0_11; -.
DR Proteomes; UP000032410; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08194; Fe-ADH-like; 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}.
FT DOMAIN 9..377
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 388 AA; 40374 MW; C8DA73337DA37A86 CRC64;
MVSNISFPRF LKLGGGAVEE LGTVLTDLDV SRPLLVTDAF MAGNGSADRL MKIMTEAGKT
PALFSGTVPD PTTDSLVAGL DAVQQHSADS IIGFGGGSPM DTAKALAILA VQGGTMRDFK
APVLSTGPAL PIIAIPTTAG SGSEATQFTI ITDVASDEKM LCPGLSFLPI ASIIDFELTM
SMPARLTADT GVDALTHAIE AYVSKKANPI SDGLALSAIR TIRTSLLRAY RDGDDRQARE
AMMHASTQAG MAFSNASVCL VHGMSRPIGA HFHVAHGLSN AMLLPAVTAF SIDGAQARYA
DCARALGAAS ESDSDQLAGG KLQDAIVTLC REVEVPTPET FGIEKAKWDQ LLPLMAEQAL
ASGSPGNNPV VPTAEQIVDL YRQVYAGI
//
