ACOX_SYNY3
ID ACOX_SYNY3 Reviewed; 490 AA.
AC P74334;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Apocarotenoid-15,15'-oxygenase;
DE Short=ACO;
DE AltName: Full=8'-apo-beta-carotenal 15,15'-oxygenase;
DE EC=1.13.11.75;
DE AltName: Full=Diox1;
GN OrderedLocusNames=sll1541;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND INDUCTION.
RX PubMed=15686550; DOI=10.1111/j.1365-2958.2004.04460.x;
RA Ruch S., Beyer P., Ernst H., Al-Babili S.;
RT "Retinal biosynthesis in Eubacteria: in vitro characterization of a novel
RT carotenoid oxygenase from Synechocystis sp. PCC 6803.";
RL Mol. Microbiol. 55:1015-1024(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP SUBSTRATE AND IRON, AND COFACTOR.
RX PubMed=15821095; DOI=10.1126/science.1108965;
RA Kloer D.P., Ruch S., Al-Babili S., Beyer P., Schulz G.E.;
RT "The structure of a retinal-forming carotenoid oxygenase.";
RL Science 308:267-269(2005).
CC -!- FUNCTION: Cleaves a number of carotenals and carotenols in the all-
CC trans configuration at the 15-15' double bond producing retinal or
CC retinol, respectively. Also shows activity toward lycopenals and the
CC corresponding alcohols. Does not cleave beta-carotene or lycopene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-8'-apo-beta-carotenal + O2 = (2E,4E,6E)-2,6-
CC dimethylocta-2,4,6-trienedial + all-trans-retinal;
CC Xref=Rhea:RHEA:26385, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:53154, ChEBI:CHEBI:53155; EC=1.13.11.75;
CC Evidence={ECO:0000269|PubMed:15686550};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:15821095};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:15821095};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for 8'-apo-beta-carotenal {ECO:0000269|PubMed:15686550};
CC KM=43 uM for 8'-apo-beta-carotenol {ECO:0000269|PubMed:15686550};
CC KM=1.4 uM for (3R)-3-OH-8'-apo-beta-carotenal
CC {ECO:0000269|PubMed:15686550};
CC KM=31 uM for (3R)-3-OH-8'-apo-beta-carotenol
CC {ECO:0000269|PubMed:15686550};
CC KM=2.6 uM for (3R)-3-OH-12'-apo-beta-carotenal
CC {ECO:0000269|PubMed:15686550};
CC Vmax=40 pmol/min/mg enzyme with 8'-apo-beta-carotenal as substrate
CC {ECO:0000269|PubMed:15686550};
CC Vmax=650 pmol/min/mg enzyme with 8'-apo-beta-carotenol as substrate
CC {ECO:0000269|PubMed:15686550};
CC Vmax=71 pmol/min/mg enzyme with (3R)-3-OH-8'-apo-beta-carotenal as
CC substrate {ECO:0000269|PubMed:15686550};
CC Vmax=705 pmol/min/mg enzyme with (3R)-3-OH-8'-apo-beta-carotenol as
CC substrate {ECO:0000269|PubMed:15686550};
CC Vmax=11.5 pmol/min/mg enzyme with (3R)-3-OH-12'-apo-beta-carotenal as
CC substrate {ECO:0000269|PubMed:15686550};
CC -!- INDUCTION: By high light. {ECO:0000269|PubMed:15686550}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18428.1; -; Genomic_DNA.
DR PIR; S76169; S76169.
DR PDB; 2BIW; X-ray; 2.39 A; A/B/C/D=1-490.
DR PDB; 2BIX; X-ray; 2.68 A; A/B=1-490.
DR PDB; 4OU8; X-ray; 2.80 A; A/B/C/D=1-490.
DR PDB; 4OU9; X-ray; 2.00 A; A/B/C/D=1-490.
DR PDB; 5KJA; X-ray; 2.80 A; A/B/C/D/E=1-490.
DR PDB; 5KJB; X-ray; 2.81 A; A/B/C/D/E=1-490.
DR PDB; 5KJD; X-ray; 2.75 A; A/B/C/D/E=1-490.
DR PDB; 5KK0; X-ray; 2.80 A; A/B/C/D=1-490.
DR PDB; 6BIG; X-ray; 2.21 A; A/B/C/D=1-490.
DR PDB; 6C7K; X-ray; 2.50 A; A/B/C/D=1-490.
DR PDB; 6C7O; X-ray; 3.15 A; A/B=1-490.
DR PDB; 6C7P; X-ray; 2.60 A; A/B=1-490.
DR PDBsum; 2BIW; -.
DR PDBsum; 2BIX; -.
DR PDBsum; 4OU8; -.
DR PDBsum; 4OU9; -.
DR PDBsum; 5KJA; -.
DR PDBsum; 5KJB; -.
DR PDBsum; 5KJD; -.
DR PDBsum; 5KK0; -.
DR PDBsum; 6BIG; -.
DR PDBsum; 6C7K; -.
DR PDBsum; 6C7O; -.
DR PDBsum; 6C7P; -.
DR AlphaFoldDB; P74334; -.
DR SMR; P74334; -.
DR IntAct; P74334; 2.
DR STRING; 1148.1653515; -.
DR DrugBank; DB02253; (1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Ol.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR PaxDb; P74334; -.
DR EnsemblBacteria; BAA18428; BAA18428; BAA18428.
DR KEGG; syn:sll1541; -.
DR eggNOG; COG3670; Bacteria.
DR InParanoid; P74334; -.
DR OMA; HHIPYGL; -.
DR PhylomeDB; P74334; -.
DR BioCyc; MetaCyc:MON-15972; -.
DR BRENDA; 1.13.11.75; 6192.
DR SABIO-RK; P74334; -.
DR EvolutionaryTrace; P74334; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0102162; F:all-trans-8'-apo-beta-carotenal 15,15'-oxygenase; IEA:UniProtKB-EC.
DR GO; GO:0010436; F:carotenoid dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; IBA:GO_Central.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Apocarotenoid-15,15'-oxygenase"
FT /id="PRO_0000387567"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15821095"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15821095"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15821095"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15821095"
FT BINDING 304
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15821095"
FT BINDING 484
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15821095"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4OU9"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4OU9"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4OU9"
FT TURN 191..195
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 198..217
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5KJD"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6C7P"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:4OU9"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:4OU9"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:6C7O"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:4OU9"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:4OU9"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:6C7O"
FT STRAND 441..449
FT /evidence="ECO:0007829|PDB:4OU9"
FT TURN 450..453
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:5KJB"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:4OU9"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:4OU9"
SQ SEQUENCE 490 AA; 54286 MW; F72AD2AAE81E6F25 CRC64;
MVTSPPTSSP SQRSYSPQDW LRGYQSQPQE WDYWVEDVEG SIPPDLQGTL YRNGPGLLEI
GDRPLKHPFD GDGMVTAFKF PGDGRVHFQS KFVRTQGYVE EQKAGKMIYR GVFGSQPAGG
WLKTIFDLRL KNIANTNITY WGDRLLALWE GGQPHRLEPS NLATIGLDDL GGILAEGQPL
SAHPRIDPAS TFDGGQPCYV TFSIKSSLSS TLTLLELDPQ GKLLRQKTET FPGFAFIHDF
AITPHYAIFL QNNVTLNGLP YLFGLRGAGE CVQFHPDKPA QIILVPRDGG EIKRIPVQAG
FVFHHANAFE ENGKIILDSI CYNSLPQVDT DGDFRSTNFD NLDPGQLWRF TIDPAAATVE
KQLMVSRCCE FPVVHPQQVG RPYRYVYMGA AHHSTGNAPL QAILKVDLES GTETLRSFAP
HGFAGEPIFV PRPGGVAEDD GWLLCLIYKA DLHRSELVIL DAQDITAPAI ATLKLKHHIP
YPLHGSWAQT
