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Database: UniProt
Entry: K9WGX5_9CYAN
LinkDB: K9WGX5_9CYAN
Original site: K9WGX5_9CYAN 
ID   K9WGX5_9CYAN            Unreviewed;       303 AA.
AC   K9WGX5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=Mic7113_3004 {ECO:0000313|EMBL:AFZ18777.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ18777.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ18777.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ18777.1,
RC   ECO:0000313|Proteomes:UP000010471};
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 Microcoleus sp. PCC 7113.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR   EMBL; CP003630; AFZ18777.1; -; Genomic_DNA.
DR   RefSeq; WP_015182926.1; NC_019738.1.
DR   AlphaFoldDB; K9WGX5; -.
DR   STRING; 1173027.Mic7113_3004; -.
DR   KEGG; mic:Mic7113_3004; -.
DR   eggNOG; COG3751; Bacteria.
DR   HOGENOM; CLU_077684_0_0_3; -.
DR   OrthoDB; 8926796at2; -.
DR   Proteomes; UP000010471; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR12907:SF26; PROLYL HYDROXYLASE EGLN3; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          149..268
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   303 AA;  35284 MW;  0F011419EB458902 CRC64;
     MEPVHQFLHQ LKQDQKLREE LAETLRVEND WNVATHIAEK YGYKFTSKKL WETIQERQQK
     GETWEDEPQP AIGVENASIQ LDNFLTAEDN HHLLEYALQH ESDFVSSLTV DLDDTLHLSP
     NHRRSLMLPS CSDVVEGVIH RIHQVLPEVR NQLLLPSFPI SGIDASLTAH NDGHFYRLHK
     DNNSIRLATR EITFVYYFCK EPKPFTGGEL RIYYNQVKKN LFAFKLIEPR NNSIVFFPSR
     YLHEILPVHC PFQNFADSRF TINGWIEQQV GSSRGANFRD LMLTLMVMIS RSQKNQMLSS
     FGT
//
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