ID A0A0Q5MK03_9MICO Unreviewed; 402 AA.
AC A0A0Q5MK03;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Alanine acetyltransferase {ECO:0000313|EMBL:KQR62952.1};
GN ORFNames=ASF89_13620 {ECO:0000313|EMBL:KQR62952.1};
OS Frigoribacterium sp. Leaf172.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR62952.1, ECO:0000313|Proteomes:UP000051720};
RN [1] {ECO:0000313|EMBL:KQR62952.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR62952.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR62952.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR62952.1,
RC ECO:0000313|Proteomes:UP000051720};
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:KQR62952.1}.
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DR EMBL; LMPB01000004; KQR62952.1; -; Genomic_DNA.
DR RefSeq; WP_055800915.1; NZ_LMPB01000004.1.
DR AlphaFoldDB; A0A0Q5MK03; -.
DR STRING; 1736285.ASF89_13620; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000051720; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase 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:SF7; ALCOHOL DEHYDROGENASE (ZN-DEPENDENT)-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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051720};
KW Transferase {ECO:0000313|EMBL:KQR62952.1};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..142
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 190..258
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 402 AA; 42226 MW; 23A6B6F9313A8CEC CRC64;
MKAVVWHGIG DIRLDEVADP AIIDPTDAVV RITRSAICGT DLHFVRGTMA PMTEGTILGH
EAVGVVTEVG DDVRGFSPGD RVVINSTVSC GSCRYCRMGQ TAQCDVANPN GPDAGTCFFG
GPASTGPVNG LQAEQVRVPF AQNTMHRLPD TVSDEQAILL SDIFPTGWFG AELAGVTRGD
VVAVFGAGVV GQFAIASAFQ QGASRVLVVD REPTRLAQAL AQNAEIVDFD EEDPVETIKR
LTGGVGVDAV IDAVGVDAQH AAHGPAAPDD ATAAEFAAEV EQVAPDADPT GDQWVPGNAP
TQALRWAVEV VAKYGRIGVI GVYSPTVTSF PFGEAMLKNL TIRMGNCDHH AVTPPLIDLV
ASGRFDPTAF ITEHEGVASA IEAYEAFDRR EPGWLKVELV AS
//
