ID A0A0A0B922_9CELL Unreviewed; 346 AA.
AC A0A0A0B922;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KGM02299.1};
GN ORFNames=Q760_14250 {ECO:0000313|EMBL:KGM02299.1};
OS Cellulomonas cellasea DSM 20118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM02299.1, ECO:0000313|Proteomes:UP000029833};
RN [1] {ECO:0000313|EMBL:KGM02299.1, ECO:0000313|Proteomes:UP000029833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM02299.1,
RC ECO:0000313|Proteomes:UP000029833};
RA Wang G., Zhuang W.;
RL Submitted (OCT-2013) 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:KGM02299.1}.
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DR EMBL; AXNT01000054; KGM02299.1; -; Genomic_DNA.
DR RefSeq; WP_034629157.1; NZ_AXNT01000054.1.
DR AlphaFoldDB; A0A0A0B922; -.
DR STRING; 1408250.Q760_14250; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000029833; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08235; iditol_2_DH_like; 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 InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 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:UP000029833};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 36310 MW; 75BE3E4B3FCDE662 CRC64;
MNVFRFYAPG DVRLEDAPEP QVGPGEVKLR VRACSMCGTD VKISTAGHQR IVPPRIMGHE
IAGEVVEVGE GVDGWVPGDR VQVIAAIPCG TCDFCTAGAM TICPNQVSMG YDFEGGFAPY
TIVPKEVLAV DGLNRIPENV SFAEASVAEP FACAINAQEI VDVHEGDDVV VVGSGPIGCL
HVRLARARGA KRVVLVELSR SRLDLASAVV NPDLAVCSAE EDPIEAVKAF FDGKGATVVI
TAAASGAAQE QGLLMLAPQG RISFFGGLPK DKPTITLDSN LVHYKELTIV GANGSSPAHN
RQALAYIADG SVPVADLITH RLPLDQIVEG IEIVRSGAGI KVTVEP
//
