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Database: UniProt
Entry: L8M2F3_9CYAN
LinkDB: L8M2F3_9CYAN
Original site: L8M2F3_9CYAN 
ID   L8M2F3_9CYAN            Unreviewed;       380 AA.
AC   L8M2F3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Putative oxidoreductase of aldo/keto reductase family {ECO:0000313|EMBL:ELS03393.1};
DE   Flags: Precursor;
GN   ORFNames=Xen7305DRAFT_00031160 {ECO:0000313|EMBL:ELS03393.1};
OS   Xenococcus sp. PCC 7305.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC   Xenococcus.
OX   NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS03393.1, ECO:0000313|Proteomes:UP000011203};
RN   [1] {ECO:0000313|EMBL:ELS03393.1, ECO:0000313|Proteomes:UP000011203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS03393.1,
RC   ECO:0000313|Proteomes:UP000011203};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELS03393.1}.
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DR   EMBL; ALVZ01000164; ELS03393.1; -; Genomic_DNA.
DR   RefSeq; WP_006509507.1; NZ_ALVZ01000164.1.
DR   AlphaFoldDB; L8M2F3; -.
DR   STRING; 102125.Xen7305DRAFT_00031160; -.
DR   PATRIC; fig|102125.3.peg.2323; -.
DR   eggNOG; COG1453; Bacteria.
DR   OrthoDB; 9773828at2; -.
DR   Proteomes; UP000011203; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd19096; AKR_Fe-S_oxidoreductase; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43312; D-THREO-ALDOSE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43312:SF2; OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011203}.
FT   DOMAIN          333..364
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   380 AA;  43506 MW;  537D29B0016DF69C CRC64;
     MQYRRFGKTN LNLSLFSLGT MRCLASPQLA ISTIKKAIAL GINHFETARG YGSSEEYLGL
     ALRSGLPIAR ENLYLTTKLP PTRDRNLMSQ WIDESLARLQ TDYLDCLAIH GINTPEHLNS
     FTQGSIQAIR QAQDQGKIRH LGFSTHGSLD LILAAIGSDL FEFVNLHYYY FWQRNQPAIA
     LAKEKDLGIF IISPGDKGGM LFTPSKTLRE LCQPWSPLEL TYRFLTSDRR ITTLSVGAAN
     PDELLFLQRE DQENQVTWSA PLTIEESWKL ETLEQHLAQK LNSDRCSQCY QCLPCPESIN
     IPEILRLRNL AVGYDMDDYG QYRYRMFENA GHWFPGKKGD RCTECGDCLP RCPENLNIPK
     LLRNTHQRLN GSPRRRLWEE
//
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