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Database: UniProt
Entry: A0A2A8S8R6_9BACI
LinkDB: A0A2A8S8R6_9BACI
Original site: A0A2A8S8R6_9BACI 
ID   A0A2A8S8R6_9BACI        Unreviewed;       307 AA.
AC   A0A2A8S8R6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Cobalamin biosynthesis protein {ECO:0000313|EMBL:PEZ04806.1};
GN   ORFNames=CN326_15750 {ECO:0000313|EMBL:PEZ04806.1};
OS   Bacillus sp. AFS018417.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ04806.1, ECO:0000313|Proteomes:UP000220085};
RN   [1] {ECO:0000313|EMBL:PEZ04806.1, ECO:0000313|Proteomes:UP000220085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ04806.1,
RC   ECO:0000313|Proteomes:UP000220085};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PEZ04806.1}.
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DR   EMBL; NTTM01000039; PEZ04806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8S8R6; -.
DR   OrthoDB; 9808822at2; -.
DR   Proteomes; UP000220085; 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:UP000220085}.
FT   DOMAIN          218..303
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   307 AA;  35300 MW;  243CF4BBEB7672F8 CRC64;
     MNKVEIHILG GFLGSGKSTL LQNLLLAEKK KNRKVAVLMN EIGEYSVDTD IVGRENILRE
     LLKGCICCTM KDELEIQLHS LYQEERPDVV YIETTGVAHP IEVLDACLSP ILAPYIEVKS
     IIVVLDAIRW LNRETLSKSV QQLLNEQMKY GSHILINKSD LLRDEEKKQV VEEVALINRH
     AKLYKTQYCN ISLEDFEEVK LASNQNHEKL HVKQHLHIQT MTYSFEKSID QGELYEWLSN
     LPEGIYRVKG FVKFHGEKYP TLLQYSFGVP SLMEQDFGFP TNLVIIGENL DKAKLKKELE
     SLEQVEL
//
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