ID F8FLK5_PAEMK Unreviewed; 380 AA.
AC F8FLK5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=AdhB3 {ECO:0000313|EMBL:AEI44132.1};
GN Name=adhB3 {ECO:0000313|EMBL:AEI44132.1};
GN OrderedLocusNames=KNP414_05608 {ECO:0000313|EMBL:AEI44132.1};
OS Paenibacillus mucilaginosus (strain KNP414).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI44132.1, ECO:0000313|Proteomes:UP000006620};
RN [1] {ECO:0000313|Proteomes:UP000006620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620};
RA Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI44132.1, ECO:0000313|Proteomes:UP000006620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNP414 {ECO:0000313|EMBL:AEI44132.1,
RC ECO:0000313|Proteomes:UP000006620};
RX PubMed=24158556;
RA Lu J.J., Wang J.F., Hu X.F.;
RT "Genome Sequence of Growth-Improving Paenibacillus mucilaginosus Strain
RT KNP414.";
RL Genome Announc. 1:e00881-13(2013).
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; CP002869; AEI44132.1; -; Genomic_DNA.
DR RefSeq; WP_013919285.1; NC_015690.1.
DR AlphaFoldDB; F8FLK5; -.
DR KEGG; pms:KNP414_05608; -.
DR PATRIC; fig|1036673.3.peg.5203; -.
DR HOGENOM; CLU_026673_11_3_9; -.
DR Proteomes; UP000006620; Chromosome.
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..144
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 191..258
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 380 AA; 41745 MW; FBD1580D54082C18 CRC64;
MRAVTYQGKK QVKVKEVQDP IIEKSDDILV RITSTAICGS DIHLVNGMVP GMPEGYVIGH
EPMGIVEEVG PEVTRVKKGD RVIIPFNVSC GECFYCKNQL ESQCDNSNDN PVYDTGAYLG
YSESYGGYAG GQAELLRVPY GNFMPFVIPP EAEVTDEQVL FLSDILPTAY WGVENSGVKP
GDTVIVLGSG PVGLLTQKFA WQKGAKRVIA VDHLDYRLYH ARNTNRVETF NFKDVDNLES
HLYEITGGGA DVVIDCVGMD GEKSVVEKLE TALKLQGGTL GPVQTARQIV RKGGTIQLIG
VYGMTYNAFP LGDLFSRNIT LKMGQAPVIH YMPELFAQIT SGKLDPTDII THRLPLTEAE
RGYEVFTDKL EDCIKVVLKP
//
