ID J1E993_9BURK Unreviewed; 354 AA.
AC J1E993;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:EJE48966.1};
GN ORFNames=PMI14_06607 {ECO:0000313|EMBL:EJE48966.1};
OS Acidovorax sp. CF316.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE48966.1, ECO:0000313|Proteomes:UP000004811};
RN [1] {ECO:0000313|EMBL:EJE48966.1, ECO:0000313|Proteomes:UP000004811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF316 {ECO:0000313|EMBL:EJE48966.1,
RC ECO:0000313|Proteomes:UP000004811};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(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:EJE48966.1}.
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DR EMBL; AKJX01000271; EJE48966.1; -; Genomic_DNA.
DR RefSeq; WP_007860959.1; NZ_AKJX01000271.1.
DR AlphaFoldDB; J1E993; -.
DR PATRIC; fig|1144317.3.peg.5999; -.
DR Proteomes; UP000004811; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
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; IPR012824; CobW.
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 NCBIfam; TIGR02475; CobW; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR PANTHER; PTHR13748:SF70; PROTEIN COBW; 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:UP000004811}.
FT DOMAIN 256..347
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
SQ SEQUENCE 354 AA; 38487 MW; 3109ED3DD3B0F37E CRC64;
MQVNKIPATI VTGFLGSGKT TLLRHLLTNA QGKRIAVIVN EFGELGIDGE LLRSCGIGCD
ENGVENGQLF ELANGCLCCT VQEEFAPVME QLAARRDQID HLVIETSGLA LPKPLVQAFQ
WPALRNVFTV DSVITVVDAP AVAAGHFADD PVAVDAQRRA DENLDHESPL HELFEDQLAT
ADLVVLHKTD GLDAEALARV EAIVRGETLP GVKFVHAQHG RIDPSVLLGL GHAVEDVIDA
RKTHHDEEED HDHDEFESVH VTLDVTDRGR LLEALVALVQ RHEIYRIKGF VALPGAAMRL
VVQGVGQRFD SHFDRAWREG DLRATRLVVI GDHLDAAALQ AELQSALAES ATTA
//
