RTPR_LACLE
ID RTPR_LACLE Reviewed; 739 AA.
AC Q59490;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE Short=RTPR;
DE EC=1.17.4.2;
GN Name=rtpR;
OS Lactobacillus leichmannii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=28039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-22; 112-121;
RP 449-461; 489-513 AND 702-739.
RX PubMed=8397403; DOI=10.1073/pnas.90.18.8352;
RA Booker S., Stubbe J.;
RT "Cloning, sequencing, and expression of the adenosylcobalamin-dependent
RT ribonucleotide reductase from Lactobacillus leichmannii.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8352-8356(1993).
RN [2]
RP PROTEIN SEQUENCE OF 112-121 AND 722-739.
RC STRAIN=ATCC 7830;
RX PubMed=3322391; DOI=10.1021/bi00396a006;
RA Lin A.-N.I., Ashley G.W., Stubbe J.;
RT "Location of the redox-active thiols of ribonucleotide reductase: sequence
RT similarity between the Escherichia coli and Lactobacillus leichmannii
RT enzymes.";
RL Biochemistry 26:6905-6909(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.0
RP ANGSTROMS) IN COMPLEX WITH ADENINYLPENTYLCOBALAMIN, AND SEQUENCE REVISION
RP TO 151.
RX PubMed=11875520; DOI=10.1038/nsb774;
RA Sintchak M.D., Arjara G., Kellogg B.A., Stubbe J., Drennan C.L.;
RT "The crystal structure of class II ribonucleotide reductase reveals how an
RT allosterically regulated monomer mimics a dimer.";
RL Nat. Struct. Biol. 9:293-300(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2;
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC -!- ACTIVITY REGULATION: Allosterically regulated by ATP and dNTP.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11875520}.
CC -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC reductase family. {ECO:0000305}.
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DR EMBL; L20047; AAA03078.1; -; Unassigned_DNA.
DR PDB; 1L1L; X-ray; 1.75 A; A/B/C/D=1-739.
DR PDBsum; 1L1L; -.
DR AlphaFoldDB; Q59490; -.
DR SMR; Q59490; -.
DR BRENDA; 1.17.4.2; 2878.
DR SABIO-RK; Q59490; -.
DR EvolutionaryTrace; Q59490; -.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR040763; RNR_alpha_hel.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF17975; RNR_Alpha; 1.
DR TIGRFAMs; TIGR02505; RTPR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cobalamin; Cobalt;
KW Direct protein sequencing; Disulfide bond; DNA replication; Oxidoreductase;
KW Redox-active center.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8397403"
FT CHAIN 2..739
FT /note="Adenosylcobalamin-dependent ribonucleoside-
FT triphosphate reductase"
FT /id="PRO_0000221428"
FT REGION 147..158
FT /note="Effector region-1"
FT REGION 168..313
FT /note="Effector region-2"
FT REGION 565..626
FT /note="Adenosylcobalamin-binding-1"
FT REGION 685..724
FT /note="Adenosylcobalamin-binding-2"
FT ACT_SITE 408
FT ACT_SITE 410
FT DISULFID 119..419
FT /note="Redox-active"
FT CONFLICT 152
FT /note="F -> C (in Ref. 1; AAA03078)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 298..313
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 396..401
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 436..450
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 458..467
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 512..536
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 551..557
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 569..578
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 583..589
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 613..616
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 623..625
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 628..641
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 655..660
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 661..667
FT /evidence="ECO:0007829|PDB:1L1L"
FT TURN 668..671
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 673..679
FT /evidence="ECO:0007829|PDB:1L1L"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 695..704
FT /evidence="ECO:0007829|PDB:1L1L"
FT HELIX 709..719
FT /evidence="ECO:0007829|PDB:1L1L"
SQ SEQUENCE 739 AA; 81983 MW; 8B04C6A5EADB6D6E CRC64;
MSEEISLSAE FIDRVKASVK PHWGKLGWVT YKRTYARWLP EKGRSENWDE TVKRVVEGNI
NLDPRLQDSP SLELKQSLTE EAERLYKLIY GLGATPSGRN LWISGTDYQR RTGDSLNNCW
FVAIRPQKYG DSKIVPSYLG KQEKAVSMPF SFLFDELMKG GGVGFSVARS NISQIPRVDF
AIDLQLVVDE TSESYDASVK VGAVGKNELV QDADSIYYRL PDTREGWVLA NALLIDLHFA
QTNPDRKQKL ILDLSDIRPY GAEIHGFGGT ASGPMPLISM LLDVNEVLNN KAGGRLTAVD
AADICNLIGK AVVAGNVRRS AELALGSNDD QDFISMKQDQ EKLMHHRWAS NNSVAVDSAF
SGYQPIAAGI RENGEPGIVN LDLSKNYGRI VDGYQAGIDG DVEGTNPCGE ISLANGEPCN
LFEVFPLIAE EQGWDLQEVF ALAARYAKRV TFSPYDWEIS REIIQKNRRI GISMSGIQDW
LLTRLGNRVV TGFKDDFDPE THEAIKVPVY DKRAIKMVDQ LYKAVVKADQ DYSKTLGCNE
SIKHTTVKPS GTVAKLAGAS EGMHFHYGAY LIQRIRFQDS DPLLPALKAC GYRTEADIYT
ENTTCVEFPI KAVGADNPNF ASAGTVSIAE QFATQAFLQT YWSDNAVSCT ITFQDSEGDQ
VESLLRQYRF ITKSTSLLPY FGGSLQQAPK EPIDKETYEK RSQEITGNVE EVFSQLNSDV
KDLELVDQTD CEGGACPIK
