ID K9VT07_9CYAN Unreviewed; 431 AA.
AC K9VT07;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:AFZ11041.1};
GN ORFNames=Cri9333_0038 {ECO:0000313|EMBL:AFZ11041.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ11041.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ11041.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ11041.1,
RC ECO:0000313|Proteomes:UP000010472};
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., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-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; CP003620; AFZ11041.1; -; Genomic_DNA.
DR RefSeq; WP_015201185.1; NC_019753.1.
DR AlphaFoldDB; K9VT07; -.
DR STRING; 1173022.Cri9333_0038; -.
DR KEGG; cep:Cri9333_0038; -.
DR PATRIC; fig|1173022.3.peg.40; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_0_1_3; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 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; 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; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000010472}.
FT DOMAIN 37..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 431 AA; 46866 MW; 195AA77EDC495BB0 CRC64;
MAIAQTLETI FNSDTSIYNW DNLDSYWQKR LTPAFPPHQT PSYILYPQSE SELAQAMAYA
YRNNEQIIVC GTGTKLGWGK STKTQLVIST SRLNHLIEHA VGDLTVTVEA GMKFAEVQNI
LAAANQFIAL DPAYPEDATI GGIIATADAG SWRQRYGGVR DMILGLTFIR ADGEIAKAGG
RVVKNVAGYD LMKLFTGSYG TLGIISQVTL RVYPLPKASA TVVLTGDKEA IATASKTLLA
SALTPTAIDL ISRQLVSQLS IGKGMGLIVR FQSVAESIQQ QSARLIEVGE HLGLHYLTYS
DDEEANLWKK LQENLWLPTQ SSDIICKIGV KPSEAVALLG DEIASSSAMG VIHATSGLGI
LRLEKPEMIP QIRSFCESKA GFLSILEAPA TVKEKLDVWG YKGNALDLMV KIKQQFDPKN
LLNPGRFVGE K
//
