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Database: UniProt
Entry: R4KI44_9FIRM
LinkDB: R4KI44_9FIRM
Original site: R4KI44_9FIRM 
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};
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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
//
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