ID A0A0J1BVF6_9MICC Unreviewed; 382 AA.
AC A0A0J1BVF6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KLU10336.1};
GN ORFNames=ABL57_07420 {ECO:0000313|EMBL:KLU10336.1};
OS Kocuria sp. SM24M-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU10336.1, ECO:0000313|Proteomes:UP000036489};
RN [1] {ECO:0000313|EMBL:KLU10336.1, ECO:0000313|Proteomes:UP000036489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU10336.1,
RC ECO:0000313|Proteomes:UP000036489};
RA Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
RL Submitted (MAY-2015) 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:KLU10336.1}.
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DR EMBL; LDNX01000061; KLU10336.1; -; Genomic_DNA.
DR RefSeq; WP_047802823.1; NZ_LDNX01000061.1.
DR AlphaFoldDB; A0A0J1BVF6; -.
DR PATRIC; fig|1660349.3.peg.3562; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000036489; 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 25..139
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 188..259
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 382 AA; 41323 MW; 7398489C3FE9C867 CRC64;
MKAMVYRGPY KVRVEEKDIP GIEHPNDAIV RVTTAAICGS DLHLYHGMMP DTRVGTTFGH
EFVGVVHEVG PSVERLKPGD RVMVPFNVYC GSCWFCARGL YSNCHNVNPN ATAVGGIYGY
SHTCGGYDGG QAEFVRVPFA DVGPSVIPDW MEEEDAVLCT DALATGYFGA QLGDIAEGDT
VVVLGAGPVG LFAAKSAWLM GAGRVIVIDH LEYRLEKARE FAQAETVNFA EHDDVVVELK
RSTDHLGADV VIDAVGAEAD GNFTQHVTSA KLKLQGGSPV ALNWAIDSVR KGGTVSVMGA
YGPMFSAVKF GDAMNKGLTL RMNQCPVKRQ WPRLFEHIRN GYLKPSDIVT HRIPLEHIAE
GYHMFSAKLD GCIKPLIVPG TS
//
