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Database: UniProt
Entry: Q1LPE2_CUPMC
LinkDB: Q1LPE2_CUPMC
Original site: Q1LPE2_CUPMC 
ID   Q1LPE2_CUPMC            Unreviewed;       397 AA.
AC   Q1LPE2;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Cobalamin synthesis protein/P47K {ECO:0000313|EMBL:ABF07984.1};
DE            EC=3.6.-.- {ECO:0000313|EMBL:ABF07984.1};
GN   Name=cobW {ECO:0000313|EMBL:ABF07984.1};
GN   OrderedLocusNames=Rmet_1098 {ECO:0000313|EMBL:ABF07984.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF07984.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC       subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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DR   EMBL; CP000352; ABF07984.1; -; Genomic_DNA.
DR   RefSeq; WP_011515885.1; NC_007973.1.
DR   AlphaFoldDB; Q1LPE2; -.
DR   STRING; 266264.Rmet_1098; -.
DR   KEGG; rme:Rmet_1098; -.
DR   eggNOG; COG0523; Bacteria.
DR   HOGENOM; CLU_017452_2_0_4; -.
DR   Proteomes; UP000002429; Chromosome.
DR   GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR   CDD; cd03112; CobW-like; 1.
DR   Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036627; CobW-likC_sf.
DR   InterPro; IPR011629; CobW-like_C.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047920; ZigA-like.
DR   NCBIfam; NF038288; chaper_GTP_ZigA; 1.
DR   PANTHER; PTHR43603; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1.
DR   PANTHER; PTHR43603:SF1; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABF07984.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT   DOMAIN          258..373
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   397 AA;  44375 MW;  C479A7CA1DE3C579 CRC64;
     MLPAKLPVTV LSGFLGAGKT TLLNHILHNR EGRRVAVIVN DMSDVNIDAG LVRDGGANLS
     RTEETLVEMS NGCICCTLRE DLLLEVERLA REGRFDQLVI ESTGISEPLP VAETFTFEGE
     DGRSLNEVAH LDTMVTVVDA FNFLRDYGSR DSLQSRGESL GEEDARTVVD LLIDQVEFCD
     VLVLNKVDLI ADADRERLLA ILRALNPRAR IEIAEFGRVP LERVLGTGLF DFEEASKAPG
     WLQEMRGQHV PETEEYGIRS FVYGARRPFH PQRFHAFVAA EWPGVVRSKG FFWLASHPTL
     AGTWSQAGAV ARHGPAGYWW AAVPPERWPD DPESVALIRA KWDDSVGDAR QEIVLIGVDM
     DEFELRRCLD ACLLTDDEMA QGPDVWTTWH NPFPDWP
//
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