ARPD_ENTAV
ID ARPD_ENTAV Reviewed; 352 AA.
AC Q8KQL2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=D-arabitol-phosphate dehydrogenase;
DE Short=APDH;
DE EC=1.1.1.301 {ECO:0000269|PubMed:12467497};
OS Enterococcus avium (Streptococcus avium).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=33945;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A DEHYDROGENASE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR,
RP ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 35665 / DSM 20063 / R 6566;
RX PubMed=12467497; DOI=10.1042/bj20021096;
RA Povelainen M., Eneyskaya E.V., Kulminskaya A.A., Ivanen D.R., Kalkkinen N.,
RA Neustroev K.N., Miasnikov A.N.;
RT "Biochemical and genetic characterization of a novel enzyme of pentitol
RT metabolism: D-arabitol-phosphate dehydrogenase.";
RL Biochem. J. 371:191-197(2003).
CC -!- FUNCTION: Involved in the arabitol catabolism via the arabitol
CC phosphate route. Catalyzes only the transformation of D-arabitol 1-
CC phosphate (Arb1P) and D-arabitol 5-phosphate (Arb5P) into D-xylulose 5-
CC phosphate (Xlu5P) and ribulose 5-phosphate, respectively. It can use
CC both NAD and NADP. {ECO:0000269|PubMed:12467497}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinitol 1-phosphate + NAD(+) = D-xylulose 5-phosphate +
CC H(+) + NADH; Xref=Rhea:RHEA:26002, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57737, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58566; EC=1.1.1.301;
CC Evidence={ECO:0000269|PubMed:12467497};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12467497};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:12467497};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, 4-hydroxymercuribenzoic acid
CC (PHMB), mercury and zinc ions at a concentration of 2 mM.
CC {ECO:0000269|PubMed:12467497}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for Xlu5P (with NAD at 20 degrees Celsius and at pH 7.2)
CC {ECO:0000269|PubMed:12467497};
CC KM=0.63 mM for Arb5P (with NAD at 20 degrees Celsius and at pH 7.2)
CC {ECO:0000269|PubMed:12467497};
CC KM=0.65 mM for Xlu5P (with NADP at 20 degrees Celsius and at pH 7.2)
CC {ECO:0000269|PubMed:12467497};
CC KM=2.9 mM for Arb1P (with NAD at 20 degrees Celsius and at pH 7.2)
CC {ECO:0000269|PubMed:12467497};
CC KM=3.6 mM for Arb1P (with NADP at 20 degrees Celsius and at pH 7.2)
CC {ECO:0000269|PubMed:12467497};
CC Vmax=0.09 umol/min/mg enzyme with Arb1P as substrate (with NADP at 20
CC degrees Celsius and at pH 7.2) {ECO:0000269|PubMed:12467497};
CC Vmax=0.15 umol/min/mg enzyme with Arb5P as substrate (with NAD at 20
CC degrees Celsius and at pH 7.2) {ECO:0000269|PubMed:12467497};
CC Vmax=1.2 umol/min/mg enzyme with Arb1P as substrate (with NAD at 20
CC degrees Celsius and at pH 7.2) {ECO:0000269|PubMed:12467497};
CC Vmax=1.2 umol/min/mg enzyme with Xlu5P as substrate (with NADP at 20
CC degrees Celsius and at pH 7.2) {ECO:0000269|PubMed:12467497};
CC Vmax=14 umol/min/mg enzyme with Xlu5P as substrate (with NAD at 20
CC degrees Celsius and at pH 7.2) {ECO:0000269|PubMed:12467497};
CC pH dependence:
CC Optimum pH is 6.8-7.3 in the reductive reaction and pH 8.3-8.6 in the
CC oxidative reaction. {ECO:0000269|PubMed:12467497};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12467497}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AY078980; AAL78068.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KQL2; -.
DR SMR; Q8KQL2; -.
DR KEGG; ag:AAL78068; -.
DR BioCyc; MetaCyc:MON-15300; -.
DR BRENDA; 1.1.1.301; 8592.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051157; P:arabitol catabolic process; IMP:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Manganese; Metal-binding; NAD; NADP; Oxidoreductase; Zinc.
FT CHAIN 1..352
FT /note="D-arabitol-phosphate dehydrogenase"
FT /id="PRO_0000418980"
FT BINDING 43
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 352 AA; 38828 MW; 3FE6AE0F20DDCB6C CRC64;
MSKTMKGVSK QAPGYDQMAF IDLSVPEATD DKVLIKVAYT GICGSDIHTF KGEYKNPTTP
VVLGHEFSGQ VVEVGANVPK VKVGDRVTSE TTFYVCGECD YCKEKQYNLC PHRKGIGTQQ
NGSMANYVLA REESIHLLPD HLSYEGAAMS EPLACCVHAM YQKSHLELKD TIIIMGPGPI
GLYLLQIAKE IGAFVIMTGI TKDAHRLALA KKLGADVIVD TMKEDLAKVV NEITDGYGVD
KVYDASGAVP AVNASLPLIR KQGQFIQVGL FANKMVDLDT ESIIQREIEY IGSRSQNPYD
WPIAIHLLAK GAINIDEMIT KKYPLTEWRE AFDKVMEGNE IKVMIESNPE EF
