ID A0ZHM5_NODSP Unreviewed; 472 AA.
AC A0ZHM5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Lignostilbene-alpha,beta-dioxygenase {ECO:0000313|EMBL:AHJ28514.1};
GN ORFNames=NSP_21820 {ECO:0000313|EMBL:AHJ28514.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ28514.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ28514.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ28514.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787}.
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DR EMBL; CP007203; AHJ28514.1; -; Genomic_DNA.
DR RefSeq; WP_006197241.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZHM5; -.
DR STRING; 313624.NSP_21820; -.
DR PATRIC; fig|313624.11.peg.2207; -.
DR eggNOG; COG3670; Bacteria.
DR HOGENOM; CLU_016472_0_2_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR PANTHER; PTHR10543:SF89; CAROTENOID 9,10(9',10')-CLEAVAGE DIOXYGENASE 1; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:AHJ28514.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 283
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 459
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 472 AA; 52859 MW; 0C3474F4F2C82637 CRC64;
MTTTEINPYL NHNFAPVRDE ITTDTLKVIG ELPANLSGMF VRNGPNPQWS PIGKYHWFDG
DGMLHGVRIS NGQATYCNRY VRTKGWKIEQ EAGKAVWSGL LEPPQMDNPH GGYKNTANTA
LVWHAGQMLA LNEGGAPHAI KLPDLQTIGE YTYNNQLVSA FTAHPKVDPK NGEMMFFGYS
FAPPYLQYSI VSAAGEIVKT VPIDLPMGVM MHDFAITENY TIFMDLPLTF SPERAQRGEP
AMMFESDVYD GLRLRPSRFG IIPRHGDNSN IRWFESSPCY VFHTLNAYED QDEIVLVACR
MSSTSVLKAD DSQTDPEADI PRLHRWRFNL STGKVQEEML DDVSAEFPRI NENLLGQATR
YGYAGRMDNS PLPLFDGLIK YDLNNGKSQT HAFKQGCYGG EAVFAPSIGA KHEDDGWLIT
FVHDEALQKS EIVVLNAQDV TAEPVARVLI PQRVPYGFHG TWVSEEQLSK TV
//
