ID R4KI44_9FIRM Unreviewed; 373 AA.
AC R4KI44;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Glycine/D-amino acid oxidase, deaminating {ECO:0000313|EMBL:AGL02284.1};
GN ORFNames=Desgi_2885 {ECO:0000313|EMBL:AGL02284.1};
OS Desulfoscipio gibsoniae DSM 7213.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfoscipio.
OX NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL02284.1, ECO:0000313|Proteomes:UP000013520};
RN [1] {ECO:0000313|EMBL:AGL02284.1, ECO:0000313|Proteomes:UP000013520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL02284.1,
RC ECO:0000313|Proteomes:UP000013520};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA Brambilla E., Spring S., Stams A.F., Woyke T.;
RT "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CP003273; AGL02284.1; -; Genomic_DNA.
DR RefSeq; WP_006520865.1; NC_021184.1.
DR AlphaFoldDB; R4KI44; -.
DR STRING; 767817.Desgi_2885; -.
DR KEGG; dgi:Desgi_2885; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_3_9; -.
DR OrthoDB; 9794226at2; -.
DR Proteomes; UP000013520; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13847:SF287; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000013520};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..351
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 373 AA; 40619 MW; AEC783D2E3EF20FA CRC64;
MNKKEIIIVG GGVIGCALAY YLTKLKIKAL VIEKNEIGIE ASSRNGGGVR QSARDLREMP
LARHAVQNLW PGLSDELGVD VEYERKGNLR LGKTEEHAKI LERIVSQGRS AGLDLKLIDR
QEVREICPYA SEEVMVASYC PTDGHANPMR TTLAFYKRAR EMGAEFVTGE TVQSILLRKG
KVGGIKTGAG TYESDQVLVA AGFASRFIAN SVGIDVPMQK VLVEALVTGQ QPPMFPQMIG
TAGSDFYGHQ TKHGSFVFGG MTGLEPFASE ESRPMTRNIT APSICRAILG YFPVLDQADI
IRTWSGFLDV TADHVPVLSK VDEIPGLFLA CGFSGHGYGI SPAVGQVMAE LVIHDRPSLS
LDAFRYDRFI PKK
//