ID B0SYS1_CAUSK Unreviewed; 487 AA.
AC B0SYS1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN OrderedLocusNames=Caul_1272 {ECO:0000313|EMBL:ABZ70402.1};
OS Caulobacter sp. (strain K31).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ70402.1};
RN [1] {ECO:0000313|EMBL:ABZ70402.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31 {ECO:0000313|EMBL:ABZ70402.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1,
CC ECO:0000256|RuleBase:RU364048};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1,
CC ECO:0000256|RuleBase:RU364048};
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787, ECO:0000256|RuleBase:RU364048}.
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DR EMBL; CP000927; ABZ70402.1; -; Genomic_DNA.
DR AlphaFoldDB; B0SYS1; -.
DR STRING; 366602.Caul_1272; -.
DR KEGG; cak:Caul_1272; -.
DR eggNOG; COG3670; Bacteria.
DR HOGENOM; CLU_016472_0_2_5; -.
DR OrthoDB; 6636843at2; -.
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:0000256|RuleBase:RU364048};
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,
KW ECO:0000256|RuleBase:RU364048}.
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 290
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 472
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 487 AA; 54328 MW; 77EA8E0DB0A7214A CRC64;
MKLDRLPPVR TSLHPTNHPY MTGAWTPLHE EVDAVDLEVL EGAIPADLDG VYLRNTENPV
HQPLGRYHPF DGDGMVHQIE FKNGAASYRN RFIRTRGFEA EQEAGESLWG GLADGPGTSR
RPGFGAHGGL KDTASTDIVV HAGEAIATFY QCGEAYRLDP LTLENLGVAA WAPLDGVSAH
AKVDEATGEL LFFNYSKHAP YMHYGVVDAN GKRTVYQPID LPGPRLPHDM AFTANYSILN
DLPVFWDQTL LERDIHAVRL HKGVPSRFGI VPRHGGEVRW FEAAPTYVLH WLNAYEDGDE
IVLDGYFQEN PTPRPLEDAP EGHGHLMAYL DEHSFRPKLH RWRFNLATGE TTEQHLDERI
LEFGMFNQAY AGRPYRYAYS TTAKPGWFLF NGFVKHDLET GESWSLALEP GRYASEAPFA
PRVGAVDEDD GYLVSFIIDE NRGTSECLVV DAKTMTPTCR IALPHKISSG THAVWAGRKM
LAPSTIP
//
