ID H0JMM4_9NOCA Unreviewed; 393 AA.
AC H0JMM4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:EHK85434.1};
GN ORFNames=AK37_03848 {ECO:0000313|EMBL:EHK85434.1};
OS Rhodococcus pyridinivorans AK37.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1114960 {ECO:0000313|EMBL:EHK85434.1, ECO:0000313|Proteomes:UP000005064};
RN [1] {ECO:0000313|EMBL:EHK85434.1, ECO:0000313|Proteomes:UP000005064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK37 {ECO:0000313|EMBL:EHK85434.1,
RC ECO:0000313|Proteomes:UP000005064};
RA Kriszt B., Tancsics A., Cserhati M., Toth A., Nagy I., Horvath B.,
RA Tamura T., Kukolya J., Szoboszlay S.;
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}.
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:EHK85434.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHBW01000030; EHK85434.1; -; Genomic_DNA.
DR RefSeq; WP_006550762.1; NZ_AHBW01000030.1.
DR AlphaFoldDB; H0JMM4; -.
DR GeneID; 29938443; -.
DR PATRIC; fig|1114960.4.peg.766; -.
DR Proteomes; UP000005064; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 1.
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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..143
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 189..258
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 393 AA; 41981 MW; 16601D0F7A9072B3 CRC64;
MKAVTWQGRR NVSVDTVPDP TIQEAGDAVI RVTTTNICGS DLHLYEVLGA FMTPGDILGH
EPMGIVEEVG SGVTNLKPGD RVVIPFQVCC GQCFMCSHGL HSQCETTQVR EEGTGAALFG
YSKLYGSVPG GQAEYLRVPH ADATHIKVPE GPADDRFVYL SDVLPTAWQA VEYAEIPDGG
SVTVLGLGPI GEMAARIAVH KGARVIGVDM VPERLARAAS RGIEVVDLRE VDNNPGDMIR
DMTNGRGTDS VIDAVGMEAH GSPVAKLAQS AAGFLPSAIA EPFMEKAGVD RLHALYTAID
VVRRGGAISL SGVYGGAADP MPMLTLFDKQ IRLHMGQANV LNWVPEILPL LTDEDPLGVD
DFATHRLPLD DAPHAYEIFQ KKQDGAIKIC LKP
//
