ID A0A195D408_9HYME Unreviewed; 744 AA.
AC A0A195D408;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=ALC62_01443 {ECO:0000313|EMBL:KYN07623.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN07623.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN07623.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN07623.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN07623.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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|ARBA:ARBA00000206,
CC 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; KQ976881; KYN07623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195D408; -.
DR STRING; 456900.A0A195D408; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000078542; 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 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.
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:UP000078542}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 744 AA; 85329 MW; BD8604F3443E02E8 CRC64;
MHVLKRDGRK EPVHFDKITA RIETLCYGLD MNYVDPSVIA LRVITNLCSG VTTIELDNLA
AETAATMINQ HPDYAILAAR IAISNLHKET KKVFSEVIAN LYHARRSITN ERFPVISEKH
YQIIQNNADK LNSAIIYDRD FNYSYATFKM LESDHLLKLN GKVVERPQHM LMRVAVAIHD
EDINKAIETY NFMSKQYFIH AEQTIDTACS VTQQMASTFL LTMSGDSIDG ILDTLERFAV
LCHHNGEVGF NVHCIRAKKT PIRGTGGVSN GLVPMLKAYN TSIATVSKNN KNEGPITVYL
EPWHSDIFEF LDLKRSIGEE QLRAKGMCYG LWTPNLFMKR VFDDDVWSLM CPHECPGLIE
TWGDKFETLY TTYEKQGRFR RQVKARDLWL LITQIQFETG VPYIVYKDHC NYKSNHQHLG
AIKCSSFSTE VVQYSSSDEV AMCNTASIAV NMFVNSTKRV FDFYKLKEIA KIVTYNLDKM
IDVNFYPLPE TKSSCDKHRS IGIGVQGLAD AFILMRYPFE SKEANELNVQ IFETLYYGAL
EASCEIANEK GPYELYEGSP ISKGILQFDM WHVKPTNLWD WDILKGKIAT HGVRNSLLIA
QMSNAFMAQM LENNISVEPY TSNIYTIYAL SKQYSVIKPH LLRDLIEKGL WDENMCNKII
LNGGSVQNIE EIPEDLRLLY KTVWEMPQKT IFEMAASRGP FIDQSQCLNI HMVDPLQKLT
SMHFYAWEIV STKYILHKLF LDYT
//
