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Database: UniProt
Entry: H1LEU4_9LACO
LinkDB: H1LEU4_9LACO
Original site: H1LEU4_9LACO 
ID   H1LEU4_9LACO            Unreviewed;       721 AA.
AC   H1LEU4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=HMPREF9104_01120 {ECO:0000313|EMBL:EHO52299.1};
OS   Lentilactobacillus kisonensis F0435.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=797516 {ECO:0000313|EMBL:EHO52299.1, ECO:0000313|Proteomes:UP000005025};
RN   [1] {ECO:0000313|EMBL:EHO52299.1, ECO:0000313|Proteomes:UP000005025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0435 {ECO:0000313|EMBL:EHO52299.1,
RC   ECO:0000313|Proteomes:UP000005025};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) 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|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   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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:EHO52299.1}.
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DR   EMBL; AGRJ01000109; EHO52299.1; -; Genomic_DNA.
DR   RefSeq; WP_008856299.1; NZ_JH591026.1.
DR   AlphaFoldDB; H1LEU4; -.
DR   STRING; 797516.HMPREF9104_01120; -.
DR   PATRIC; fig|797516.3.peg.996; -.
DR   HOGENOM; CLU_000404_4_1_9; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000005025; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:UniProtKB-UniPathway.
DR   CDD; cd01679; RNR_I; 1.
DR   Gene3D; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR026459; RNR_1b_NrdE.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013554; RNR_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR   PANTHER; PTHR11573:SF30; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005025}.
FT   DOMAIN          558..580
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   721 AA;  82225 MW;  8EE2CAB18A9AE55E CRC64;
     MSLHNLTDTS YFDLNNEINI PVNGQIPLQK DQEALQAFLD KNVGPNLVKF DSLKARFNYL
     VANNYYEKDF INKYDFDFIE KLYSYLQSQD FHFKSFMAAY KFYAQYALKT NDNDSYLETF
     LDRVAVNALY FADGNEDLAM ALADEIIHQR YQPATPSFLN AGRENRGEFV SCFLIQTTDD
     MNTIGRTINS ALQLSRIGGG VGINLSNLRA AGDPIKHIEG AASGVVPVMK LLEDSFSYSN
     QLGQRQGAGV VYLSVFHPDI ISFLGAKKEN ADEKIRLKTL SLGITVPDKF YELIKADADM
     YLFSPYDVER EYGKPFSYID ITKEYDRLVA NDNIKKTKIK ARDLETEISK LQQESGYPYI
     INIDTANRVN PIDGRIVMSN LCSEILQVQT PSTVDNEQHY IKLGKDISCN LGSTNINNMM
     NSTHFGHSIE TMVRALTYVT DHSNIDVVPS IQKGNHESHS IGLGAMGLHS FFAKHHMHYG
     SPESIEFTST YFMLLNYWSL VASNKIARER HKTFDNFEKS KYADGTYFDK YFENSYAPKS
     DKVKALFTND MIPTKEDWQA LKESVMKYGL YHQNRLAVAP NGSISYINDT TASLHPIINR
     IEERQESKIG KIYYPAPYLS NDTMPYYTSA YDMDMRKVID IYAAAQEHID QGMALTLFMR
     STIPAGLYEW KDGRTNKMTT RDLNILRNYA HKKGVKSIYY IRTFTDDQQE VGSNQCESCV
     I
//
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