ID Y015_SYNE7 Reviewed; 223 AA.
AC Q31SC2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=PKHD-type hydroxylase Synpcc7942_0015 {ECO:0000255|HAMAP-Rule:MF_00657};
DE EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN OrderedLocusNames=Synpcc7942_0015;
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP000100; ABB56047.1; -; Genomic_DNA.
DR RefSeq; WP_011243792.1; NZ_CP130602.1.
DR AlphaFoldDB; Q31SC2; -.
DR SMR; Q31SC2; -.
DR STRING; 1140.Synpcc7942_0015; -.
DR PaxDb; 1140-Synpcc7942_0015; -.
DR GeneID; 76398763; -.
DR KEGG; syf:Synpcc7942_0015; -.
DR eggNOG; COG3128; Bacteria.
DR HOGENOM; CLU_106663_0_0_3; -.
DR OrthoDB; 9812472at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0015-MONOMER; -.
DR Proteomes; UP000889800; 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 Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 4.10.860.20; Rabenosyn, Rab binding domain; 1.
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; PKHD-TYPE HYDROXYLASE YBIX; 1.
DR PANTHER; PTHR41536:SF1; PKHD-TYPE HYDROXYLASE YBIX; 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..223
FT /note="PKHD-type hydroxylase Synpcc7942_0015"
FT /id="PRO_0000346525"
FT DOMAIN 78..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 223 AA; 25186 MW; 527D7265BF3D4B2A CRC64;
MIITIDALLD AAQLNKIQSS LQTAEFIDGR ATAGWHAQLV KQNQQLSRTS TLAKSLQEIV
QTALQNNALF EAAAYPQRVH SLLFSRYEPG MEYGRHVDNA LMGSGDRRDR ADLSFTLFLS
DPDRYIGGAL VIEGACDEQA YRLPAGSLLL YPSSTLHRVD PVEQGYRFAC VGWVQSWIRD
PAKRELLFDL DTARRSLFTR EGKSIEFDLL SKTYANLLRR WSE
//
