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Database: UniProt
Entry: I4N182_9PSED
LinkDB: I4N182_9PSED
Original site: I4N182_9PSED 
ID   I4N182_9PSED            Unreviewed;       317 AA.
AC   I4N182;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Cobalamin synthesis protein/P47K {ECO:0000313|EMBL:EIK95222.1};
GN   ORFNames=PMM47T1_18485 {ECO:0000313|EMBL:EIK95222.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK95222.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK95222.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK95222.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(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:EIK95222.1}.
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DR   EMBL; AJWX01000017; EIK95222.1; -; Genomic_DNA.
DR   RefSeq; WP_008371620.1; NZ_AJWX01000017.1.
DR   AlphaFoldDB; I4N182; -.
DR   STRING; 1179778.PMM47T1_18485; -.
DR   PATRIC; fig|1179778.3.peg.3697; -.
DR   eggNOG; COG0523; Bacteria.
DR   OrthoDB; 9808822at2; -.
DR   Proteomes; UP000004339; 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   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   PANTHER; PTHR13748:SF62; COBW DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13748; COBW-RELATED; 1.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 1.
DR   SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004339}.
FT   DOMAIN          223..317
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   317 AA;  34977 MW;  03B5DDEE4EF0FD70 CRC64;
     MSSPIPVTIL SGFLGAGKTT LLRHLLKAEH GLKIAVIENE FSDAGIDTQL LGDAPVQVMT
     LANGCVCCTI HTDLTKALYL LMERLDSGEI AFDRLVIECT GLADPAPVAQ TFFIDEELRE
     RYILDGIITL VDAANAEVHL AQTIAQAQVG FADRLLVSKT DLVSPHAFEA LSERLTRINR
     RAPIRVVRHG EIDLAELLDV RGFNLNGSLN VRPVVAADSL DRISSMVLRT EQPLDIDKLS
     AFMNQLLEDH GRQLLRYKGV LNIAGEDRRL VFQGVLKLYG FDWDTEWSEG EVRESVMVFI
     ADDLPEATIR AGFNALT
//
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