LAADH_SYNY3
ID LAADH_SYNY3 Reviewed; 471 AA.
AC Q55629;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=L-amino acid dehydrogenase {ECO:0000303|PubMed:19213808};
DE EC=1.4.5.- {ECO:0000305|PubMed:19213808};
DE AltName: Full=L-amino acid:plastoquinone oxidoreductase {ECO:0000303|PubMed:19213808};
DE AltName: Full=L-arginine dehydrogenase {ECO:0000303|PubMed:19213808};
GN OrderedLocusNames=slr0782;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INDUCTION, AND
RP PATHWAY.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=19213808; DOI=10.1093/jxb/ern352;
RA Schriek S., Kahmann U., Staiger D., Pistorius E.K., Michel K.P.;
RT "Detection of an L-amino acid dehydrogenase activity in Synechocystis sp.
RT PCC 6803.";
RL J. Exp. Bot. 60:1035-1046(2009).
CC -!- FUNCTION: L-amino acid dehydrogenase with broad substrate specificity.
CC Catalyzes the oxidative deamination of various L-amino acids, L-Arg and
CC L-Cys being the best substrates in vitro. Likely functions mainly as an
CC L-arginine dehydrogenase in vivo. Probably feeds electrons from L-
CC arginine oxidation and also from the oxidation of other L-amino acids
CC into the respiratory electron transport chain associated to the
CC thylakoid membrane, and does not directly interact with molecular
CC oxygen but donates electrons to the plastoquinone pool. Cannot use D-
CC amino acids as substrates. {ECO:0000269|PubMed:19213808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + an L-alpha-amino acid + H2O = a 2-
CC oxocarboxylate + a plastoquinol + NH4(+); Xref=Rhea:RHEA:53020,
CC Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17757, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000305|PubMed:19213808};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + H2O + L-arginine = 5-guanidino-2-
CC oxopentanoate + a plastoquinol + NH4(+); Xref=Rhea:RHEA:53024,
CC Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17757, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58489, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000305|PubMed:19213808};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9S3V1};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q9S3V1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9S3V1};
CC -!- ACTIVITY REGULATION: Inhibited by Ca(2+) and other cations such as
CC Ni(2+), Co(2+) and Zn(2+). The inhibition by o-phenanthroline and
CC salicylhydroxamic acid suggests the presence of a metal cofactor
CC besides FAD in the enzyme. The L-arginine-stimulated O(2) consumption
CC involving slr0782 is inhibited by inhibitors of the respiratory
CC electron transport chain, such as KCN and 2,5-dibromo-3-methyl-6-
CC isopropyl-p-benzoquinone, which indicates a participation of the
CC cytochrome b6/f complex and of a cytochrome oxidase.
CC {ECO:0000269|PubMed:19213808}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 mM for L-arginine {ECO:0000269|PubMed:19213808};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation.
CC {ECO:0000305|PubMed:19213808}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:19213808}.
CC -!- INDUCTION: Up-regulated when cells are grown with L-arginine as
CC compared to the growth of cells with nitrate (at mRNA and protein
CC level). The increase is substantially higher in the PsbO-free mutant
CC than in wild-type. {ECO:0000269|PubMed:19213808}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA10142.1; -; Genomic_DNA.
DR PIR; S76290; S76290.
DR AlphaFoldDB; Q55629; -.
DR SMR; Q55629; -.
DR STRING; 1148.1001515; -.
DR PaxDb; Q55629; -.
DR EnsemblBacteria; BAA10142; BAA10142; BAA10142.
DR KEGG; syn:slr0782; -.
DR eggNOG; COG1231; Bacteria.
DR InParanoid; Q55629; -.
DR OMA; PIHWAGT; -.
DR PhylomeDB; Q55629; -.
DR BRENDA; 1.4.1.5; 382.
DR UniPathway; UPA00073; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Thylakoid.
FT CHAIN 1..471
FT /note="L-amino acid dehydrogenase"
FT /id="PRO_0000099869"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
FT BINDING 60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
FT BINDING 256
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
FT BINDING 453
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9S3V1"
SQ SEQUENCE 471 AA; 51404 MW; F534F45D9FB1117B CRC64;
MVIRSGKTNL NPPCALMAPS SSCDCIIVGS GLSGLIAARN LSRVNYSVLV IEAQERLGGR
MYGEYLPSGQ WIDRGGQWVG PTQDRFLALL NEYNIERFPS PADGLKVLLF DGKRYEFDGF
FQGVFQGEAP KISSDEWNDA MVAWEKFNTL AQSLDEQHPE ATPENKKLDS QTFADWIKEN
THTAFGHWYF SYMCRAVGFL GPAEPSQVSL LHILWGHKSA SQGENPEAEL LHGGAGQIPQ
KIAAELGNSI LLGEPVIHIA QDDKGVEVTT TTGKYQGKFA IVATPPHLAG RITYSPPMPP
LRQQLTQRVP MGTCCKLLIS YDRPFWREKG LAGIGLGNTT WIELCADSSD PTTGVGVIAS
FVVGDRYGKW IAMGEAERRQ GVLSDLALYF GEEALSPETY DEVDWPSEQW VGGGYAAFMP
PGVWTSFGQA LSAPVGRIHW AGTEIAPRWA GFFDGAIRTG EAAAKAIIGL L
