ID A0A0Q5C278_9MICO Unreviewed; 391 AA.
AC A0A0Q5C278;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Molecular chaperone GroES {ECO:0000313|EMBL:KQQ25435.1};
GN ORFNames=ASF54_13460 {ECO:0000313|EMBL:KQQ25435.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ25435.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ25435.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ25435.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ25435.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ25435.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQQ25435.1}.
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DR EMBL; LMNV01000005; KQQ25435.1; -; Genomic_DNA.
DR RefSeq; WP_055964143.1; NZ_LMNV01000005.1.
DR AlphaFoldDB; A0A0Q5C278; -.
DR STRING; 1736329.ASF54_13460; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000051456; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000051456};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..140
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 189..255
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 391 AA; 41994 MW; 5092CBBE974D123A CRC64;
MRALTYQAVT KVSVEEVPDP TIIEPTDAVI RVTSAAICGS DLHLYDALGP YLDKGDVLGH
ETMGVVTAVG TEVSRIKVGD RVVVPFVIAC GHCFMCDRGL FSQCETTQVT EYDSGATLYG
FSKLYGQTPG GQAEQLRIQR ADFNLITVGA TLPDERYLFL SDILPTAWQG VEYAEVPDGG
TLVVLGLGPV GQFASRIGVH KGYRVIAVDP VPERRTMAER HGVETLDLTD DVSAIIKKMT
DDRGPDSVLD AVGMEAHEHG AVGLFQKMAG VLPDAVGQAV MQKAGIDSLG AMHLAFDVVR
RGGTVSLSGV YGGTADPTPF LNLFDKQISL RMGQCNVQKW TETLMPLVED PADPLGTEDL
VTHPVPLEQA AEMYDLFKTK GDGCIKVVLK P
//
