ID K9PSE1_9CYAN Unreviewed; 371 AA.
AC K9PSE1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=D-amino-acid:oxygen oxidoreductase (Deaminating) {ECO:0000313|EMBL:AFY35477.1};
DE EC=1.4.3.3 {ECO:0000313|EMBL:AFY35477.1};
GN ORFNames=Cal7507_5135 {ECO:0000313|EMBL:AFY35477.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY35477.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY35477.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY35477.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000189-1};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003943; AFY35477.1; -; Genomic_DNA.
DR RefSeq; WP_015131268.1; NC_019682.1.
DR AlphaFoldDB; K9PSE1; -.
DR STRING; 99598.Cal7507_5135; -.
DR KEGG; calo:Cal7507_5135; -.
DR PATRIC; fig|99598.3.peg.5752; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_034311_4_0_3; -.
DR OrthoDB; 246701at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF25; FAD DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00677; DAO; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW Oxidoreductase {ECO:0000313|EMBL:AFY35477.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390}.
FT DOMAIN 4..352
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 40..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 336..341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 371 AA; 41474 MW; 3B24BD4D30B27E04 CRC64;
MQARVLVIGG GVSGLTTALC LLQDGFAVTV VSEKFAPNNT SVVAGALWEW PPAVCGSHRH
PVSLERSKSW CMVSYNKFLN LAANKETGVY NRDVVFYYKK PIEQTLELQK MNELQMRVLR
FRRDKTLIDW YGINRDTGVV DAYTYLAPQV DTDIYMQWLY SQVKESGCKI VEAKISGNLA
EIQEQLKSQF SVDIIVNCSG LGSIELTNDD MYPLRGALIR VKNDGVSMPR VTTSHCMTFD
NSVGGQNMIF ILPRGEKTLL LGGLVEPDKW ELDINLENYE PIQDMWNRCL NFMPSLKDAT
IDAAEPVRVG LRPGRKDNIR LERELGTDII HNYGHGGSGV TLSWGCAQEV VQIVKSRTGA
QEVVQMANSR A
//
