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Database: UniProt
Entry: H1SH06_9BURK
LinkDB: H1SH06_9BURK
Original site: H1SH06_9BURK 
ID   H1SH06_9BURK            Unreviewed;       570 AA.
AC   H1SH06;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Cobalamin synthesis protein/P47K {ECO:0000313|EMBL:EHP38197.1};
GN   ORFNames=OR16_38499 {ECO:0000313|EMBL:EHP38197.1};
OS   Cupriavidus basilensis OR16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP38197.1, ECO:0000313|Proteomes:UP000005808};
RN   [1] {ECO:0000313|EMBL:EHP38197.1, ECO:0000313|Proteomes:UP000005808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR16 {ECO:0000313|EMBL:EHP38197.1,
RC   ECO:0000313|Proteomes:UP000005808};
RX   PubMed=22461549; DOI=10.1128/JB.06752-11;
RA   Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA   Nagy I., Horvath B., Nagy I., Kukolya J.;
RT   "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL   J. Bacteriol. 194:2109-2110(2012).
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}.
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:EHP38197.1}.
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DR   EMBL; AHJE01000140; EHP38197.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1SH06; -.
DR   PATRIC; fig|1127483.3.peg.7668; -.
DR   Proteomes; UP000005808; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   Gene3D; 2.40.50.870; Protein of unknown function (DUF3299); 1.
DR   InterPro; IPR036627; CobW-likC_sf.
DR   InterPro; IPR011629; CobW-like_C.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR021727; DUF3299.
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   Pfam; PF11736; DUF3299; 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}.
FT   DOMAIN          431..546
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   570 AA;  62491 MW;  FEC09B418B1E892E CRC64;
     MVKETGMTPR VQRALFALTV IAVATAGAVY VFRSLPPPEP RAEAAAAVPP AYATGEAPQP
     ASAPAAPDPA LRQIEWQALL PKGWDPLAPF KGMKLDELED GDPRAQIALY KARQYWKNAP
     VEPTLDGAAV RIAGFVVSLD GEGESIREFL LVPYFGACIH VPPPMPSPMP SPMPSPTLLP
     VTVLSGFLGA GKTTLLNHIL HNRQGRRVAV IVNDMSEVNI DAALVRDGGA GLSRTDERLV
     EMSNGCICCT LREDLLVEVR RLAKEGRFDQ LVIESTGISE PLPVAETFTF TDEDGQSLSQ
     VARLDTMVTV VDAYNFLRDY SSRDSLRQRG ESLGEQDGRT VVDLLVEQVE FCDVLLVNKL
     DLVGDAEREQ LMAILRGLNP RARIEPSAFG KVGLEKVLGT GLFDFEQAAN TPGWLMALRG
     EPTPETAEYG IASFVYRARR PFHPRRFFDL AEREWPGVVR SKGFFWLAAR PTRAGSWSQA
     GAICRHGPAG YWWATVPREF WPEDPDAVAT IRSHWHDDTG DARQELVLIG IGMDESALCQ
     QLDHCLLSDA EMAQGPIAWA AYDDPFPAWG
//
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