ID A0A2Z5YUP5_9SPHN Unreviewed; 493 AA.
AC A0A2Z5YUP5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN ORFNames=AEB_P0968 {ECO:0000313|EMBL:BBC71836.1};
OS Altererythrobacter sp. B11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=2060312 {ECO:0000313|EMBL:BBC71836.1, ECO:0000313|Proteomes:UP000263119};
RN [1] {ECO:0000313|EMBL:BBC71836.1, ECO:0000313|Proteomes:UP000263119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11 {ECO:0000313|EMBL:BBC71836.1,
RC ECO:0000313|Proteomes:UP000263119};
RA Maeda A.H., Nishi S., Ishii S., Shimane Y., Kobayashi H., Ichikawa J.,
RA Kurosawa K., Arai W., Takami H., Ohta Y.;
RT "Complete Genome Sequence of Altererythrobacter sp. Strain B11, an Aromatic
RT Monomer-Degrading Bacterium, Isolated from Deep-Sea Sediment under the
RT Seabed off Kashima, Japan.";
RL Genome Announc. 6:e00200-18(2018).
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; AP018498; BBC71836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5YUP5; -.
DR KEGG; alb:AEB_P0968; -.
DR OrthoDB; 6636843at2; -.
DR Proteomes; UP000263119; 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:SF37; CAROTENOID CLEAVAGE DIOXYGENASE 7, CHLOROPLASTIC; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|RuleBase:RU364048, ECO:0000313|EMBL:BBC71836.1};
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|RuleBase:RU364048};
KW Reference proteome {ECO:0000313|Proteomes:UP000263119}.
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 476
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 493 AA; 55668 MW; 59333634BE42D633 CRC64;
MAQFPDTPNF TGFNTPSRVE ADIKDLQHTG TIPPELDGAF FRVQPDPQFP PMLGDDIAFN
GDGMISRFHF HDGQCDFRQR WAQTDKWKAE RAAGRGLYGK YRNPLTDDPS VKGSIRSTAN
TNAWIFAGKL WAMKEDSPAL LMDPVTMETE GFEKFGGKMT GQTFTAHPKI DPHTGNMVAI
GYAASGLCSE DVTYYEVNPE GELVREVWFK VPYYCMMHDF GVTEDYLVLH IVPSIGSWER
LEKGLPHFGF DTTMPVYLGV IPRRDDVRDE DIRWFKRDNC FASHVLNAWQ EGTKIHFVVP
EAKNNMFPFF PDVHGAPFNG VEAMSKLTDW VVDLASNGED FAEINRLTDT ASEFPRIDDR
YTGLKNRYGW GLEMDMSRPN ELRGGSAGGF LMNCLFLKDL ETGAEQHWWC GPVSSLQEPC
FIPRSKDAPE GDGWIVMVCN RLEDHRSDLL LFDALDIEKG PIATIQVPIR LRFGLHGNFA
RSEDIGLKVP EPA
//
