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Database: UniProt
Entry: A0A0S2K982_9GAMM
LinkDB: A0A0S2K982_9GAMM
Original site: A0A0S2K982_9GAMM 
ID   A0A0S2K982_9GAMM        Unreviewed;       465 AA.
AC   A0A0S2K982;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=FAD linked oxidase, C-terminal domain protein {ECO:0000313|EMBL:ALO44793.1};
GN   ORFNames=PS2015_96 {ECO:0000313|EMBL:ALO44793.1};
OS   Pseudohongiella spirulinae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudohongiellaceae; Pseudohongiella.
OX   NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO44793.1, ECO:0000313|Proteomes:UP000065641};
RN   [1] {ECO:0000313|EMBL:ALO44793.1, ECO:0000313|Proteomes:UP000065641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO44793.1,
RC   ECO:0000313|Proteomes:UP000065641};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR   EMBL; CP013189; ALO44793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2K982; -.
DR   STRING; 1249552.PS2015_96; -.
DR   KEGG; pspi:PS2015_96; -.
DR   PATRIC; fig|1249552.3.peg.98; -.
DR   Proteomes; UP000065641; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065641}.
FT   DOMAIN          39..218
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   465 AA;  51081 MW;  67EE5498012E3EA4 CRC64;
     MSLMQQSLVA SLAEIVGPDR VKTDSESLQV FGKDWTKAHE PRPVAVVLPG STEEVQALVR
     FANEQKIALV PSGGRTGLSG AAVAANGEVV VAFDRMNKIL DFNPVDRQVV CQPGVITEQL
     QQYAEDKGLY YPVDFASSGS SQLGGNVGTN AGGIKVIRYG LTRDWVMGMK VVTGTGELLD
     LNQGLVKNAT GYDLRHLFIG SEGTLGFIVE LTMGLATQPQ DPTVLVLALE EMEASMHVLQ
     AFQAKIEVSA FEFFSEKALR HVIAEKGLAR PFETEGNFYT LIEFENTSEA TMDAAMSVFE
     HCMEQGWVLD GTMSQNVTQA KALWRLREDI SETISRFTPY KNDISVQVSK VPAFLKEVDA
     IVTSQYPDFE IIWFGHIGDG NVHLNILKPD SLAKEEFFRQ CGEVSYDIFD AVKSYGGSVS
     AEHGVGLLKK PYLHYSRSEA EIALMRGIKS LFDPNNIMNP GKIFD
//
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