ODH_ARTSC
ID ODH_ARTSC Reviewed; 359 AA.
AC Q44297;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Opine dehydrogenase;
DE EC=1.5.1.28;
DE AltName: Full=N-(1-D-carboxyethyl)-L-norvaline dehydrogenase;
GN Name=odh;
OS Arthrobacter sp. (strain 1C).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=79670;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7487048; DOI=10.1128/aem.61.8.3169-3171.1995;
RA Dairi T., Asano Y.;
RT "Cloning, nucleotide sequencing, and expression of an opine dehydrogenase
RT gene from Arthrobacter sp. strain 1C.";
RL Appl. Environ. Microbiol. 61:3169-3171(1995).
RN [2]
RP CHARACTERIZATION.
RX PubMed=2753861; DOI=10.1128/jb.171.8.4466-4471.1989;
RA Asano Y., Yamaguchi K., Kondo K.;
RT "A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain
RT 1C.";
RL J. Bacteriol. 171:4466-4471(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9665174; DOI=10.1038/854;
RA Britton K.L., Asano Y., Rice D.W.;
RT "Crystal structure and active site location of N-(1-D-carboxylethyl)-L-
RT norvaline dehydrogenase.";
RL Nat. Struct. Biol. 5:593-601(1998).
CC -!- FUNCTION: In the forward direction acts also on secondary amine
CC dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-
CC carboxyethyl)phenylalanine. In the reverse direction, the enzyme also
CC acts on neutral amino acids as an amino donor. They include L-amino
CC acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-
CC aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine,
CC isoleucine, valine, phenylalanine, leucine and alanine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-[(R)-1-carboxyethylamino]pentanoate + H2O + NAD(+) =
CC H(+) + L-2-aminopentanoate + NADH + pyruvate; Xref=Rhea:RHEA:21592,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58441,
CC ChEBI:CHEBI:58799; EC=1.5.1.28;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; D45211; BAA08145.1; -; Genomic_DNA.
DR PIR; I39664; I39664.
DR PDB; 1BG6; X-ray; 1.80 A; A=1-359.
DR PDBsum; 1BG6; -.
DR AlphaFoldDB; Q44297; -.
DR SMR; Q44297; -.
DR KEGG; ag:BAA08145; -.
DR EvolutionaryTrace; Q44297; -.
DR GO; GO:0047129; F:opine 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; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003421; Opine_DH.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF02317; Octopine_DH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase.
FT CHAIN 1..359
FT /note="Opine dehydrogenase"
FT /id="PRO_0000179982"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:1BG6"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 228..246
FT /evidence="ECO:0007829|PDB:1BG6"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1BG6"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:1BG6"
FT TURN 341..345
FT /evidence="ECO:0007829|PDB:1BG6"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:1BG6"
SQ SEQUENCE 359 AA; 37937 MW; 7542D8A44D859028 CRC64;
MIESKTYAVL GLGNGGHAFA AYLALKGQSV LAWDIDAQRI KEIQDRGAII AEGPGLAGTA
HPDLLTSDIG LAVKDADVIL IVVPAIHHAS IAANIASYIS EGQLIILNPG ATGGALEFRK
ILRENGAPEV TIGETSSMLF TCRSERPGQV TVNAIKGAMD FACLPAAKAG WALEQIGSVL
PQYVAVENVL HTSLTNVNAV MHPLPTLLNA ARCESGTPFQ YYLEGITPSV GSLAEKVDAE
RIAIAKAFDL NVPSVCEWYK ESYGQSPATI YEAVQGNPAY RGIAGPINLN TRYFFEDVST
GLVPLSELGR AVNVPTPLID AVLDLISSLI DTDFRKEGRT LEKLGLSGLT AAGIRSAVE
