TADH_ARAIR
ID TADH_ARAIR Reviewed; 397 AA.
AC Q8T882;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Tauropine dehydrogenase {ECO:0000303|PubMed:8840516};
DE Short=TaDH {ECO:0000303|PubMed:8840516};
DE EC=1.5.1.23 {ECO:0000269|PubMed:8840516};
DE AltName: Full=NAD: tauropine oxidoreductase {ECO:0000303|PubMed:8840516};
GN Name=tadh {ECO:0000312|EMBL:BAB86769.1};
OS Arabella iricolor (Opal worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Errantia; Eunicida; Oenonidae; Arabella.
OX NCBI_TaxID=65494;
RN [1] {ECO:0000312|EMBL:BAB86769.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Body wall {ECO:0000269|PubMed:15565272};
RX PubMed=15565272; DOI=10.1007/s10126-004-2700-6;
RA Kimura T., Nakano T., Yamaguchi T., Sato M., Ogawa T., Muramoto K.,
RA Yokoyama T., Kan-No N., Nagahisa E., Janssen F., Grieshaber M.K.;
RT "Complementary DNA cloning and molecular evolution of opine dehydrogenases
RT in some marine invertebrates.";
RL Mar. Biotechnol. 6:493-502(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-35, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8840516; DOI=10.1016/0305-0491(96)00072-7;
RA Kanno N., Sato M., Nagahisa E., Sato Y.;
RT "Tauropine dehydrogenase from the sandworm Arabella iricolor (Polychaeta:
RT Errantia): purification and characterization.";
RL Comp. Biochem. Physiol. 114:409-416(1996).
CC -!- FUNCTION: May play a role in maintaining a redox balance during
CC environmental and functional hypoxia. Exhibits high specificity for
CC taurine and in addition, requires both alpha amino group and C-2 carbon
CC chain length as a critical factor for active site binding of the amino
CC acid. A methyl group in the beta position may be critical for active
CC site binding of the keto acid. In the reverse reaction requires NAD(H)
CC for the activity but not NADP(H). {ECO:0000269|PubMed:8840516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + tauropine = H(+) + NADH + pyruvate + taurine;
CC Xref=Rhea:RHEA:12580, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57779,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:507393; EC=1.5.1.23;
CC Evidence={ECO:0000269|PubMed:8840516};
CC -!- ACTIVITY REGULATION: Subject to substrate inhibition by pyruvate for
CC the reverse reaction but not for the forward reaction of the tauropine
CC dehydrogenase activity. {ECO:0000269|PubMed:8840516}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35.7 mM for taurine for the reverse reaction of the tauropine
CC dehydrogenase activity (at pH 7.0) {ECO:0000269|PubMed:8840516};
CC KM=0.34 mM for pyruvate for the reverse reaction of the tauropine
CC dehydrogenase activity (at pH 7.0) {ECO:0000269|PubMed:8840516};
CC KM=0.036 mM for NADH for the reverse reaction of the tauropine
CC dehydrogenase activity (at pH 7.0) {ECO:0000269|PubMed:8840516};
CC KM=4.9 mM for oxaloacetate for the reverse reaction of the tauropine
CC dehydrogenase activity (at pH 7.0) {ECO:0000269|PubMed:8840516};
CC KM=3.3 mM for 2-ketobutyrate for the reverse reaction of the
CC tauropine dehydrogenase activity (at pH 7.0)
CC {ECO:0000269|PubMed:8840516};
CC KM=4.8 mM for tauropine for the forward reaction of the tauropine
CC dehydrogenase activity (at pH 8.5) {ECO:0000269|PubMed:8840516};
CC KM=0.051 mM for NAD(+) for the forward reaction of the tauropine
CC dehydrogenase activity (at pH 8.5) {ECO:0000269|PubMed:8840516};
CC pH dependence:
CC Optimum pH is 8.5 for the forward reaction, and 6.6-7.3 for the
CC reverse reaction. The half-maximal rate is observed at 6.8 for the
CC forward reaction, and at 5.5-7.9 for the reverse reaction.
CC {ECO:0000269|PubMed:8840516};
CC -!- SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine
CC dehydrogenases family. {ECO:0000255}.
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DR EMBL; AB081841; BAB86769.1; -; mRNA.
DR PIR; A59226; A59226.
DR AlphaFoldDB; Q8T882; -.
DR SMR; Q8T882; -.
DR KEGG; ag:BAB86769; -.
DR BioCyc; MetaCyc:MON-18217; -.
DR BRENDA; 1.5.1.23; 400.
DR GO; GO:0050325; F:tauropine dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003421; Opine_DH.
DR Pfam; PF02317; Octopine_DH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8840516"
FT CHAIN 2..397
FT /note="Tauropine dehydrogenase"
FT /id="PRO_0000413626"
SQ SEQUENCE 397 AA; 43229 MW; 00A0CCB3B7D747C0 CRC64;
MVVLTICGGG NAAHTLAGIA SNQPNMEVRV LTLYADEAER WIKSMETNDF TTIKYATGKD
PVHLKTKPKL VTKNPEQGAT GADIIVITVP AFAHAQYLTA LKPHVKPGTV VVGFPGQPGF
DFEIMKIWGD LAKQCTVMNF VSLPWACRIK EFGKSVEVLA TKDMMFGSVR NGTVAPKMDP
TAMIQGCLGP LPRLECSGHL LGMSIMAVNG MLHPSIMYNR WHDWDGKPVD APPLFYHGLS
QAGADLLSDV SNETIAIAKK VMEQRQGVDL SNVIHMHPYY IGAYPDDISD KSSLYTCINT
NAGFKGLTHP CTKTADGKFV PDFTGRYFGE DIPFGLAVTR GIAEIAGCPT PNIDKIIEWA
QKLMGKEYLV GGKFTGKDIS ATRAPQRYGF NTLDSIL
