ID G8RXQ4_MYCRN Unreviewed; 366 AA.
AC G8RXQ4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Theronine dehydrogenase-like Zn-dependent dehydrogenase {ECO:0000313|EMBL:AEV75667.1};
GN OrderedLocusNames=MycrhN_5192 {ECO:0000313|EMBL:AEV75667.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV75667.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV75667.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV75667.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP003169; AEV75667.1; -; Genomic_DNA.
DR RefSeq; WP_014213408.1; NC_016604.1.
DR AlphaFoldDB; G8RXQ4; -.
DR STRING; 710685.MycrhN_5192; -.
DR KEGG; mrh:MycrhN_5192; -.
DR PATRIC; fig|710685.3.peg.5213; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_11; -.
DR OMA; GEYRRCE; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000005442; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 29..142
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 189..321
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 366 AA; 38395 MW; AB9B8FFD9E4043BF CRC64;
MIAEAMVLTG PRSLQRRQMT IPDVGDRGAI LRVEACGLCG TDHEQFTGHL PAGFSFVPGH
EIVGIVEHVG TSASQRWGVQ AGQRVAVEVF RSCRDCPECR RGEYRRCAVN GIATMFGFVD
VQIGAGLWGG YATHVELPWD AMLLPIAEDM DPVLATLFNP LGAGIQWGAT LPDTKAGDVV
AILGPGIRGI CAAVAAKEAG AAFVAMTGVG PRDEQRLAIA RSFGVDLPID VSQDNAVTAL
QRETGGQLAD VVVDVTAKAP SAFADAVDLA RPGSTVVVAG TRGGGGAPGF EPDLLVYKEL
RVVGALGVEY PAYRAALEIL AEGRWPFDRI TRESTGFAGL APLLNSLADE NARSSAALHN
VFLPTP
//