ID K9RMX1_9CYAN Unreviewed; 446 AA.
AC K9RMX1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=FAD-linked oxidoreductase {ECO:0000313|EMBL:AFY58649.1};
GN ORFNames=Riv7116_6302 {ECO:0000313|EMBL:AFY58649.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY58649.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY58649.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY58649.1,
RC ECO:0000313|Proteomes:UP000010380};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005147}.
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DR EMBL; CP003549; AFY58649.1; -; Genomic_DNA.
DR RefSeq; WP_015122198.1; NC_019678.1.
DR AlphaFoldDB; K9RMX1; -.
DR STRING; 373994.Riv7116_6302; -.
DR KEGG; riv:Riv7116_6302; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_003896_4_3_3; -.
DR OrthoDB; 9800184at2; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_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; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR01679; bact_FAD_ox; 1.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 4: Predicted;
KW Ascorbate biosynthesis {ECO:0000256|ARBA:ARBA00022644};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000010380}.
FT DOMAIN 13..183
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 446 AA; 51250 MW; 963D2A8FF86FDF54 CRC64;
MNQERFINWS GEYQCTPNYV HHPVSNEEVK DIVCQAIKRG SKIRVFGSGH SPSDMAMSNE
ELVCLDGLNA IKNIHAENQT VVVEAGVTIN ELSQSLAKYG LALPNLGSIS AQTISGAMAT
ATHGTGLNYG TMPTIIEEIT LVNGKGEIIK VSQTENSQFF NAVKCHLGSL GLITEYKLKV
TKSFDLEVQE QPQTLAAVFE NLPESLKSDH YRFWYLPHVD MAWEWTATRK PPEESTVKGK
NIFQRLGDWY QQQLIGFYTF QFLLYIATYD QNLIPRINRW YAQQMFSKPK QSRGDSLSQF
NFDCLFKQQV NEWAIPIEYT VQALEAIRDL IQKKDYKAHL PIEVRFVKGD DIWLSPCQGR
DSCYIGIINY MPYGKRVDCQ DYFNDYEKIM TKFNGRPHWA KRFGPDAKEL AKIYPHWNDF
MQVRYQLDPD NRFGNSYSDR VLGQMG
//