ID A0A0M2H131_9MICO Unreviewed; 537 AA.
AC A0A0M2H131;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aryl-alcohol dehydrogenase {ECO:0000313|EMBL:KJL40123.1};
DE EC=1.1.1.90 {ECO:0000313|EMBL:KJL40123.1};
GN Name=xylB_2 {ECO:0000313|EMBL:KJL40123.1};
GN ORFNames=RS81_01713 {ECO:0000313|EMBL:KJL40123.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL40123.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL40123.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL40123.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL40123.1}.
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DR EMBL; JYIZ01000047; KJL40123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2H131; -.
DR STRING; 92835.RS81_01713; -.
DR PATRIC; fig|92835.4.peg.1732; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000033956; Unassembled WGS sequence.
DR GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 1.
DR Gene3D; 2.40.128.580; GXWXG domain; 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; IPR025568; DUF4334.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR025951; GXWXG_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF14232; DUF4334; 1.
DR Pfam; PF14231; GXWXG; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 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 ECO:0000313|EMBL:KJL40123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..357
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 364..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 55535 MW; 456D453C775C18A4 CRC64;
MGADVAAIVR GRGGAPVLES VSVSPPRAGE VLVRVLASGV CHTDLVAIDG GIGYPFPAVF
GHEGAGIVEA VGEGVTRVHP GDRVVLSFAS CGTCAACRSG HPAYCELFGS LNHSPETGAM
AVEATGEALN AGFMRQSSWA TRVLAHESNT VPIPADVPAT VAAPLGCGVL TGAATVLNVL
SPTAGDDLVV IGAGAVGLSA VMAARASGCR SIIVSDPLPA RRDLALDLGA TAAVGPDGLA
EAIAAGGPVR HVIDTVGTQE TTDAALAALA PRGTVATVAL RPGSNRVSIA QGRLLWGRTI
TGVIEGDAVV QRDIPRLVDL WHAGLLPVER IVTAYGLDEI ERAVDDTRAG RAVKAVLVTP
EAASEATRRA ADTASAPVAD RPTDAGEPVG LLFTLRARTL DDAGLARLWR SLPPVEPAEL
RGLWRGWAVT TGHRAERMLA RSGWYGKRFH SDSEVDPIVV RTGDGELVAD ETFSHGGASL
WRIERDGVLT VAMVYDALPI VDSFTRITPD AVLGVMGGKN TADEGREFYF VLERDAD
//
