ID V2UUL1_9GAMM Unreviewed; 943 AA.
AC V2UUL1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=P255_00427 {ECO:0000313|EMBL:ESK52276.1};
OS Acinetobacter brisouii CIP 110357.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK52276.1, ECO:0000313|Proteomes:UP000018418};
RN [1] {ECO:0000313|EMBL:ESK52276.1, ECO:0000313|Proteomes:UP000018418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK52276.1,
RC ECO:0000313|Proteomes:UP000018418};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
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:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|RuleBase:RU364064}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406}.
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:ESK52276.1}.
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DR EMBL; AYEU01000003; ESK52276.1; -; Genomic_DNA.
DR RefSeq; WP_004903160.1; NZ_KI530762.1.
DR AlphaFoldDB; V2UUL1; -.
DR STRING; 396323.VH98_11830; -.
DR PATRIC; fig|1341683.3.peg.420; -.
DR HOGENOM; CLU_000404_3_0_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000018418; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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:0071897; P:DNA 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; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR02504; NrdJ_Z; 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; 2.
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}; Cobalamin {ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000018418}.
FT DOMAIN 11..111
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 122..211
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 943 AA; 105206 MW; 20F87CE808BEA799 CRC64;
MSVISSTPGQ LQVIKRTGDV VHFDAEKISV AIGKAFLAVE GQQSADSSRI HDRIAQLTEM
VMNTFHRRLP SGGTIHIEEI QDQVELALMR TGEQKVARAY VIYREQRATA RQQTNANHHP
TLQILDAQGQ LQPLDLTELT ATITKAAEGL EGIDVQAIVD ETVKNLYNGV KASDIATTMM
MATRTRIEQE PNYTYVTARL LCNELVATGL EFLGLPTDTP ESDALETFLK KGIELELLDP
ELLNFDLAKL AAAIQPERSN QFTYLGLQTL FDRYFIHSDG VRYELPQLFF MRVAMGLALN
EDNREDRAIE FYNLLSSFDY MASTPTLFNA GTLRPQLSSC YLTTISDDLY SIYGAIRDNA
MLSKWAGGLG NDWTPVRALN SYIKGTNGKS QGVVPFLKVA NDTAVAVNQG GKRKGAVCAY
LETWHLDIEE FLELRKNTGD DRRRTHDMNT ANWVPDLFMQ RVIEDAEWTL FTPSDVPDLH
DLTGNAFVER YTHYENIAKE LNLLHKKVRA KDLWRKMLSM LFETGHPWIT FKDVCNLRSP
QQHVGVVHSS NLCTEITLNT SEDEIAVCNL GSVNLVQHVQ GGVLDREKLA RTIKTAVRML
DNVIDINYYA VPQAKNSNMK HRPVGMGIMG FQDALYEMGM AYGSQEAVDF ADESMEVISY
YAIQTSSDLA VERGVYSTFK GSLWDQGILP IDSLEIVAKS RPERMFEVDR TQRLDWNSLR
AKVQKDGMRN SNVMAIAPTA TISNICGVSQ SIEPTFQNLY VKSNLSGEFT VINPYLVRAL
KARGLWDSVM VNDLKHFEGS VQKISRIPED LKAMFSTAFE VEPRWIVDAA SRRQKWIDQA
QSLNLYIAGA NGKKLDITYK MAWLRGLKTT YYLRALGATS AEKSTINTGA LNAVKPATVA
AAVAAPVVAE KKAEVVAEEE GFSQAAPVPQ ACSIDNPDCE ACQ
//
