ID A0A1M3M404_9PROT Unreviewed; 334 AA.
AC A0A1M3M404;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:OJX80863.1};
GN ORFNames=BGO92_07100 {ECO:0000313|EMBL:OJX80863.1};
OS Magnetospirillum sp. 64-120.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX80863.1, ECO:0000313|Proteomes:UP000184435};
RN [1] {ECO:0000313|EMBL:OJX80863.1, ECO:0000313|Proteomes:UP000184435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=64-120 {ECO:0000313|EMBL:OJX80863.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJX80863.1}.
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DR EMBL; MKVK01000011; OJX80863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3M404; -.
DR STRING; 1895778.BGO92_07100; -.
DR Proteomes; UP000184435; 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}.
FT DOMAIN 243..334
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
SQ SEQUENCE 334 AA; 35832 MW; 0F15D10C95C5A1C6 CRC64;
MRKVPATVIT GFLGAGKTTL VRHLMENNQG RRIALIVNEF GDVGVDGDLL ASCGVAGCQE
DDIIELANGC LCCTVADEFL PTMQALLDRP NPPDHILIET SGLALPKPLV KAFHWPEIRT
RVTVDGVLAV VDGAAVAAGR FADTPEMMAQ PGHDNPLEEV FEDQLACADM VLLNKTDLLD
GGALDATHAE LSAKLRPGVR VIRTSRSAID PIVALGLSAA AEDDLAQRPS HHDTEDGHDH
DDFESFAVSL PEVADPAALE AKLITVIAAH DILRLKGFLA VSGKPARHVV QAVGTRIERW
FDRPWKGDEQ RQSRLVVIGE KGLDRAAIET AILA
//
