ID A3YTZ8_9SYNE Unreviewed; 509 AA.
AC A3YTZ8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Lignostilbene-alpha,beta-dioxygenase and related enzyme-like {ECO:0000313|EMBL:EAQ76512.1};
GN ORFNames=WH5701_04555 {ECO:0000313|EMBL:EAQ76512.1};
OS Synechococcus sp. WH 5701.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ76512.1, ECO:0000313|Proteomes:UP000002935};
RN [1] {ECO:0000313|EMBL:EAQ76512.1, ECO:0000313|Proteomes:UP000002935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH5701 {ECO:0000313|Proteomes:UP000002935};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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:EAQ76512.1}.
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DR EMBL; AANO01000001; EAQ76512.1; -; Genomic_DNA.
DR RefSeq; WP_006173132.1; NZ_CH724160.1.
DR AlphaFoldDB; A3YTZ8; -.
DR eggNOG; COG3670; Bacteria.
DR HOGENOM; CLU_016472_6_3_3; -.
DR OrthoDB; 6636843at2; -.
DR Proteomes; UP000002935; Unassembled WGS sequence.
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 InterPro; IPR011048; Haem_d1_sf.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR PANTHER; PTHR10543:SF37; CAROTENOID CLEAVAGE DIOXYGENASE 7, CHLOROPLASTIC; 1.
DR Pfam; PF03055; RPE65; 1.
DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:EAQ76512.1};
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:0000313|EMBL:EAQ76512.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002935}.
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 313
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 502
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 509 AA; 54722 MW; 6E0F54E456FABECD CRC64;
MTIAPSRPEP GKAAAASSPG YDRADWASAF RNVGTELTSV PLAAASGTIP SELSGSLYRN
GPGRLERGGR WVHHPFDGDG MITAVRFEGG AAELSNRFVR TEGWLAEEKA GKVLYRGVFG
SQKPGGPLAN AFDLRLKNIA NTHVVRLGEK LLALWEASSP HSLDPTSLET EGVELLGGVL
ADGEAFSAHP RFDPGHHGQQ RMVTFGVKAG LRSTIRLMEF DASPGAAAGT LVADQKRSFN
GFAFLHDFAI TQNWAVFLQN AMSFNPLGFV LGWKGAAQCL DSKPGERGQF WLIPRSGDGE
PLQVSAPEGF VFHHLNAFED PSAGTAGQVV VDSIFYDDFP SIGPGVDFRA VDFDSLPIGQ
LKRCRIDLAS GEVSTELLEE RCCEFAMVNP RRVGLEARYA WMAVTEQERG NAPLQAIEKL
DLSNGERLVW SAAPRGFVSE PVMVPRPRQD AEGDQPAEDD GWILCVVWNG ARCASDLVIL
NAADLSEQAV LPMPLALPHG LHGSWAAAA
//
