ID S2JWB0_MUCC1 Unreviewed; 788 AA.
AC S2JWB0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=HMPREF1544_09113 {ECO:0000313|EMBL:EPB84125.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB84125.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KE124048; EPB84125.1; -; Genomic_DNA.
DR AlphaFoldDB; S2JWB0; -.
DR STRING; 1220926.S2JWB0; -.
DR VEuPathDB; FungiDB:HMPREF1544_09113; -.
DR eggNOG; KOG1112; Eukaryota.
DR InParanoid; S2JWB0; -.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000014254; 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:UP000014254}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 788 AA; 89640 MW; 0DFA5A7ED7945DEA CRC64;
MFVYKRDGRR EKVAFDKITA RINKLCYGLD MNYVDPVAIT QKVISGVYQG VTTIELDNLA
AETAAYMTTT HPDYAQLAAR IAISNLHKET KKVFSQVVED LYTYINPKTD KHSPMIAEDI
YNIIMANAER LNSAIIYDRD FKYNFFGFKT LERSYLLKIN GKVAERPQHL IMRVAVGIHG
EDIDAAIETY NLMSERYFTH ASPTLFNAGT PRPQLSSCFL LTMKEDSIEG IYETLKICAQ
ISKTAGGIGL NIHNVRATGS YIAGTNGYSN GLLPMLRVFN NTARYVDQGG NKRPGAFAMY
LEPWHADIFM FLDLRKNFGK DEIRARDLFY ALWVPDLFME RVRDNGEWSL FCPNEAPGLC
EVWGDEFKAL FEKYEREGRA RETIKAQKLW YAILEAQTET GNPFMLYKDA CNRKSNQQNL
GTIKCSNLCT EIVEYSSPDE VAVCNLASIA LPSFVVNREK YDFQKLHDVT KVITKNLNKI
IDVNYYPVIE AERSNKRHRP IGLGVQGLAD AFMLMKFAFD SPEAKKLNIQ IFETIYHAAL
EASNELAEQL GPYETYQGSP VSQGILQYDM WNVTPTSLWD WTSLKEKIAK HGVRNSLLVA
PMPTASTSQI MGFNECFEPY TSNLYTRRVL AGEFQIVNPW LLKDLVEMDL WNEDVKNMIM
SDGGSIQNIP GIPQNLKDIY KTVWELSQRT LVDMAADRGA FIDQSQSLNI FIGEPNFGKL
TSMHFYGWQK GLKTGMYYLR TRPAVDAIKF TVDQLSLREY RKKKTEEENA ADMVCSIDNK
DACVSCSG
//
