Y1907_THEVB
ID Y1907_THEVB Reviewed; 224 AA.
AC Q8DHN8;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=PKHD-type hydroxylase tll1907 {ECO:0000255|HAMAP-Rule:MF_00657};
DE EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN OrderedLocusNames=tll1907;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00657};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC09459.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000039; BAC09459.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_682697.2; NC_004113.1.
DR RefSeq; WP_011057744.1; NC_004113.1.
DR AlphaFoldDB; Q8DHN8; -.
DR SMR; Q8DHN8; -.
DR STRING; 197221.22295633; -.
DR EnsemblBacteria; BAC09459; BAC09459; BAC09459.
DR KEGG; tel:tll1907; -.
DR PATRIC; fig|197221.4.peg.1993; -.
DR eggNOG; COG3128; Bacteria.
DR OMA; FPPLFNC; -.
DR OrthoDB; 1139586at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00657; Hydroxyl_YbiX; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR041097; PKHD_C.
DR InterPro; IPR023550; PKHD_hydroxylase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR41536; PTHR41536; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF18331; PKHD_C; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Vitamin C.
FT CHAIN 1..224
FT /note="PKHD-type hydroxylase tll1907"
FT /id="PRO_0000206684"
FT DOMAIN 77..176
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 167
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ SEQUENCE 224 AA; 25357 MW; 0BB602823FA5626D CRC64;
MLLQIDRVLT TEELNQLNTL LQAGVFEDGK WTAGIYAKTV KDNQQLVQEG EEYRVASEIV
LSALSRNQLF QAYVQPKIIG PLLFSRYEVG MAYGTHTDNA LMGSGDQLRR SDVSLTIFLN
DPFAYEGGAL VLDTSLGEQY FKLPAGSMIV YPSIFLHRVE TVSKGVRLVA VAWVQSLIRD
PLERELLFEL DTVRRSLFEK QGKTVDFDLL CKVYSNLLRK WAEI
