DADA_CERS4
ID DADA_CERS4 Reviewed; 436 AA.
AC Q3IXK6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=D-amino acid dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01202};
DE EC=1.4.99.- {ECO:0000255|HAMAP-Rule:MF_01202};
GN Name=dadA {ECO:0000255|HAMAP-Rule:MF_01202}; OrderedLocusNames=RHOS4_31600;
GN ORFNames=RSP_3113;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000255|HAMAP-
CC Rule:MF_01202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 +
CC NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59871; Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
CC -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC pyruvate from D-alanine: step 1/1.
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR EMBL; CP000144; ABA80728.1; -; Genomic_DNA.
DR RefSeq; WP_011339050.1; NZ_CP030272.1.
DR RefSeq; YP_354629.1; NC_007494.2.
DR AlphaFoldDB; Q3IXK6; -.
DR SMR; Q3IXK6; -.
DR STRING; 272943.RSP_3113; -.
DR EnsemblBacteria; ABA80728; ABA80728; RSP_3113.
DR KEGG; rsp:RSP_3113; -.
DR PATRIC; fig|272943.9.peg.3539; -.
DR eggNOG; COG0665; Bacteria.
DR OMA; FWYKEDG; -.
DR PhylomeDB; Q3IXK6; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002703; Chromosome 2.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0055130; P:D-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01202; DadA; 1.
DR InterPro; IPR023080; DadA.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..436
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066112"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 436 AA; 46151 MW; CAE52B673FC38B0B CRC64;
MRIVVLGAGV VGVTSAYELA RAGHEVTVVD RQPAAALETS FANAGEISPG YASPWAAPGI
PAKALRWMFM KHAPLVIRPR LDAAQVRFLL AILRNCTPAA YAQNKGRMVR LAEYSRDCLT
DLRATTGLAF DERQQGTLQL FRSQKQLDAA ARDIEVLRAG GVPFELLDAD GCLAAEPGLR
AARDRIAGGL RLTGDETGDC FKFTQGLAGL AEEGGVRFRY GTGVERLRVE GGRVTGVETT
KGTFLADAVV VALGSHSPAL VAPLGLRLPV YPVKGYSITV PIVDADRAPV STVMDETYKI
AITRLGTRIR VGGMAEVAGF SATLPPARRE TLAMSVNDLF GGAGDLSRAS FWTGLRPMTP
DGTPVVGRTP VAGLWLNTGH GTLGWTMAAG SARVLSDLID GRAPEIESAD LGIERYAAPG
RRARPAVRLN PARQAG
