ID A0A1V6T584_9EURO Unreviewed; 866 AA.
AC A0A1V6T584;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=PENSTE_c012G07900 {ECO:0000313|EMBL:OQE21079.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE21079.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|ARBA:ARBA00024942,
CC ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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:OQE21079.1}.
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DR EMBL; MLKD01000012; OQE21079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6T584; -.
DR STRING; 303698.A0A1V6T584; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000191285; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 822..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 96404 MW; D1B2847EDEAC714A CRC64;
MFVYKRDGRK ERVQFDKITA RVSRLCYGLD PEHVDAAAIT QKVISGVYQG VGTIELDNLA
AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQFSMVISD LYHYVNPKNS KPAPMISKNI
YEIVTKHADE LNSAIVYDRD FNYNFFGFKT LERSYLLRID GKVAERPQHL LMRVAVGIHG
EDIEKAIETY HLMSQKYFTH ASPTLFNAGT PQPQLASCFL VDMKEDSIEG IYDTLKTCAM
ISKTAGGIGL NIHRIRATGS YIGGTNGTSN GIVPMLRVYN NTARYVDQGG NKRPGAFAIY
LEPWHADVFE FLDLRKNHGK EEIRARDLFY ALWTPDLFMK RVEANGDWTL FCPNEAPGLA
DVYGDEFEAL YERYEKEGRG RSTIKAQKLW YAILEAQTET GNPFMLYKDA CNKKSNQKNL
GTIRSSNLCT EIIEYSAPDE VAVCNLASLA LPTFVDASRG EYDFGKLHEV VQVLVRNLNK
IIDINYYPVQ EAKNSNFRHR PIALGVNGLA DAFLALRLPF DSPEAKQLNI QIFETIYHGA
LTASSALAKE HGPYQTYAGS PVSQGILQYD MWDRTPTDLW DWASLKAKIA ETGVRNSLLV
APMPTASTSQ ILGFNECFEP YTSNIYSRRV LAGEFQVVNP WLLKDLVDLG LWSDNMKNRI
IADGGSVQNI PNIPADIKSL YKTVWEISQR SILQMAADRG AYIDQSQSLN IHLKEPTMGK
LTSMHFAGWK MGLKTGMYYL RTMAASAPIQ FTVDQEQLKV EDTNVARANP SFKKRAVGSA
SSAYSAVPRT NGAEAATAAI NAPVQESPRT LVQETTTVVA APAAEAPAAE SKEATEQTEK
TEGDIYSDAV LQCSIENKEA CLMCQG
//
