ID Q2S7M4_HAHCH Unreviewed; 182 AA.
AC Q2S7M4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN OrderedLocusNames=HCH_06724 {ECO:0000313|EMBL:ABC33350.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC33350.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC33350.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC33350.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; CP000155; ABC33350.1; -; Genomic_DNA.
DR RefSeq; WP_011400402.1; NC_007645.1.
DR AlphaFoldDB; Q2S7M4; -.
DR STRING; 349521.HCH_06724; -.
DR KEGG; hch:HCH_06724; -.
DR eggNOG; COG3128; Bacteria.
DR HOGENOM; CLU_041456_2_0_6; -.
DR OMA; HNDSLTW; -.
DR OrthoDB; 269774at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF207; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 88..178
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 182 AA; 21109 MW; 8BA81AD4E7CA8171 CRC64;
MKKIEYGAGV FAIQGFLTAH ECDAYISDSE AMGYDEAEIQ TARGSQMYKD IRNNDRVIFD
DAVMANNIFN RIEAMLPQEL DGWELVGLNE RLRFYRYEPG QYFKWHRDGS YARSEKEASL
LSFLIFLNED YEGGEIAFRW DKIKPERGSV VVFPHAMMHQ GTTVESGVKY VLRTDVMYRE
IA
//