ID A0A0L0S6K7_ALLM3 Unreviewed; 600 AA.
AC A0A0L0S6K7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=AMAG_05048 {ECO:0000313|EMBL:KNE58238.1};
OS Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS macrogynus).
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE58238.1, ECO:0000313|Proteomes:UP000054350};
RN [1] {ECO:0000313|EMBL:KNE58238.1, ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE58238.1,
RC ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Allomyces macrogynus ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA Lander E., Nusbaum C.;
RT "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; GG745332; KNE58238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0S6K7; -.
DR STRING; 578462.A0A0L0S6K7; -.
DR EnsemblFungi; KNE58238; KNE58238; AMAG_05048.
DR VEuPathDB; FungiDB:AMAG_05048; -.
DR eggNOG; KOG3844; Eukaryota.
DR OMA; GWYHIPQ; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000054350; Unassembled WGS sequence.
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:UP000054350};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 169..275
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 65537 MW; 6F37DC378C94D0EE CRC64;
MTNPTSPTNE HDEARPAKRA RTAASATTTS AIPAVAPAMP ALPQRPPELD AATVAACFTE
GLFNEDYVQH LANNYKASHP YLHCVMHPLV REDLLRAVRA EIMGQLHFTE KETDIYKVNQ
TGDLANIDGL PLAERAALGH LHKLRNAFYS EPFRNFVSAV TGCGPLSGSK QDMSINNYRQ
GCHLLNHDDV IGTRRVSYIL YLPPPDEEWK VEYGGALELY PCVKKGTPAT DPTVVLPPKY
NQFIFFTVQP GYSFHSVQEV VVPNDRLSIS GWFHVPQDGE DGYQPMDVVL GPDAAPASLA
QLEEDAAADN DETSEYPYRP VSTDEDLTAD LSDADRAYLA QFLHPQYLTP AAMTKMNDQF
CDESSLQLRD FFKPEIASTL APLLNQADAR DRLANGDAKA LAHGAGVRAG WAVQGSPVKQ
RFMVLTGDSA ASTESPECAP LRAAADLLVS PAFARWLYHV TGIAARGTRH RVRRFRPGLD
YTLAAYSSTS ATLDVTVALT PSPRTAWEEG EIGGYECYVA PDESNDDPAV YRAAGGNEND
EDGGALLTVP ADWNVLSLVL RDQGVMRFVK YVSGLAPGSR WDIAMEVLPV PDEEDAEDAE
//
