PED_AROAE
ID PED_AROAE Reviewed; 249 AA.
AC Q5P5I4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=(S)-1-Phenylethanol dehydrogenase;
DE EC=1.1.1.311;
GN Name=ped; OrderedLocusNames=AZOSEA13030; ORFNames=c1A58;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-27, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=EbN1;
RX PubMed=11479712; DOI=10.1007/s002030100303;
RA Kniemeyer O., Heider J.;
RT "(S)-1-phenylethanol dehydrogenase of Azoarcus sp. strain EbN1, an enzyme
RT of anaerobic ethylbenzene catabolism.";
RL Arch. Microbiol. 176:129-135(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, BIOTECHNOLOGY, AND SUBUNIT.
RC STRAIN=EbN1;
RX PubMed=16388583; DOI=10.1021/bi051596b;
RA Hoffken H.W., Duong M., Friedrich T., Breuer M., Hauer B., Reinhardt R.,
RA Rabus R., Heider J.;
RT "Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol
RT dehydrogenase of the denitrifying bacterium strain EbN1.";
RL Biochemistry 45:82-93(2006).
CC -!- FUNCTION: Catalyzes the NAD-dependent stereospecific oxidation of (S)-
CC 1-phenylethanol to acetophenone in the degradation of ethylbenzene.
CC {ECO:0000269|PubMed:11479712, ECO:0000269|PubMed:16388583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-1-phenylethanol + NAD(+) = acetophenone + H(+) + NADH;
CC Xref=Rhea:RHEA:28198, ChEBI:CHEBI:15378, ChEBI:CHEBI:16346,
CC ChEBI:CHEBI:27632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.311; Evidence={ECO:0000269|PubMed:11479712,
CC ECO:0000269|PubMed:16388583};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for (S)-1-phenylethanol {ECO:0000269|PubMed:11479712};
CC KM=51 uM for NAD(+) {ECO:0000269|PubMed:11479712};
CC KM=1 uM for acetophenone {ECO:0000269|PubMed:11479712};
CC KM=3.3 uM for NADH(+) {ECO:0000269|PubMed:11479712};
CC Vmax=1.4 umol/min/mg enzyme with (S)-1-phenylethanol as substrate
CC {ECO:0000269|PubMed:11479712};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16388583}.
CC -!- BIOTECHNOLOGY: The reverse reaction is of biotechnological interest for
CC the specific production of chiral alcohols from ketones.
CC {ECO:0000269|PubMed:16388583}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CR555306; CAI07428.1; -; Genomic_DNA.
DR RefSeq; WP_011237148.1; NC_006513.1.
DR PDB; 2EW8; X-ray; 2.10 A; A/B/C/D=1-249.
DR PDB; 2EWM; X-ray; 2.40 A; A/B=1-249.
DR PDBsum; 2EW8; -.
DR PDBsum; 2EWM; -.
DR AlphaFoldDB; Q5P5I4; -.
DR SMR; Q5P5I4; -.
DR STRING; 76114.c1A58; -.
DR EnsemblBacteria; CAI07428; CAI07428; c1A58.
DR KEGG; eba:c1A58; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_4; -.
DR OMA; VGTLGKQ; -.
DR OrthoDB; 1601931at2; -.
DR BioCyc; MetaCyc:MON-1364; -.
DR BRENDA; 1.1.1.311; 12182.
DR SABIO-RK; Q5P5I4; -.
DR EvolutionaryTrace; Q5P5I4; -.
DR Proteomes; UP000006552; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0010130; P:anaerobic ethylbenzene catabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11479712"
FT CHAIN 2..249
FT /note="(S)-1-Phenylethanol dehydrogenase"
FT /id="PRO_0000418749"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT BINDING 17..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT BINDING 61..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT BINDING 89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT BINDING 184..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16388583"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:2EW8"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2EW8"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:2EW8"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:2EW8"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:2EW8"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:2EW8"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 152..172
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2EW8"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:2EWM"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:2EW8"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2EW8"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:2EW8"
SQ SEQUENCE 249 AA; 26662 MW; 2CA2967B5B6B32C4 CRC64;
MTQRLKDKLA VITGGANGIG RAIAERFAVE GADIAIADLV PAPEAEAAIR NLGRRVLTVK
CDVSQPGDVE AFGKQVISTF GRCDILVNNA GIYPLIPFDE LTFEQWKKTF EINVDSGFLM
AKAFVPGMKR NGWGRIINLT STTYWLKIEA YTHYISTKAA NIGFTRALAS DLGKDGITVN
AIAPSLVRTA TTEASALSAM FDVLPNMLQA IPRLQVPLDL TGAAAFLASD DASFITGQTL
AVDGGMVRH
