ID A0A179G592_METCM Unreviewed; 649 AA.
AC A0A179G592;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OAQ72531.1};
GN ORFNames=VFPPC_00482 {ECO:0000313|EMBL:OAQ72531.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ72531.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ72531.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ72531.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000256|ARBA:ARBA00001792};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the TPA1 family.
CC {ECO:0000256|ARBA:ARBA00007443}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAQ72531.1}.
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DR EMBL; LSBJ02000001; OAQ72531.1; -; Genomic_DNA.
DR RefSeq; XP_018148614.1; XM_018280491.1.
DR AlphaFoldDB; A0A179G592; -.
DR STRING; 1380566.A0A179G592; -.
DR GeneID; 28844485; -.
DR KEGG; pchm:VFPPC_00482; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000078397; Chromosome 1.
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:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
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:UP000078397};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 142..267
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..618
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 72808 MW; 2D6F0B1D435959FD CRC64;
MKRKAESPNG QEASTKKSKP SLSSEEAQKR FRSGLFDKSA LDSYTEEYAT SAPYKHAVIH
ELVDDKLLRS VRDEVRNNVQ FTPKETDIYK IHQSGDLANL DGLDDESLSK LPSLLALRDA
IYSETFRDYV SGITGCGPLS GRKTDMAINV YTPGCFLLCH DDVIGSRRVS YILYLTDPDK
PWKPEWGGAL RLFPVQEIES KDGEVAKTPL PDCVKVIPPA WNQLSFFAVQ PGESFHDVEE
VYHAQTKEQL DEDNGRVRMA ISGWFHIPQV GEDGYIEGEE EKNAKNSSLM QLQGNPAQYD
APQAKPVKVE NLNSSGDEFE EADLEFLLKY IAPTYLTPDT LDQISEHFSE NSSITLSDIL
SRKFAQRLKD YIEEQEKQSL PQDSETIEKS TPWQVSKPPH KHRYLYQRPS QPDQLRTSQE
ESPITELLDI LLPSRQFRHW LQVATGLTIE SHDLMARRFR RGGDYTLATG YQGEPRLEIG
LGMTPTPGWG DEVEQKDKDK DSQVNGKGKG KAKASGEKSK KDEDDVGGVE VYMAGDDDED
EDEDAAVYKS SNDDDNILFF QAAAWNKMTV VLRDSGALKF VKYVSRRAKG DRWDISGTFD
IQELEGDDEE EDGEQEEGNG EGGSGPAVDK SDDEDAFTAF AEPEESDSD
//
