ID A0A0Q5VFW7_9CAUL Unreviewed; 357 AA.
AC A0A0Q5VFW7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:KQS56491.1};
GN ORFNames=ASG17_03140 {ECO:0000313|EMBL:KQS56491.1};
OS Brevundimonas sp. Leaf363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS56491.1, ECO:0000313|Proteomes:UP000051182};
RN [1] {ECO:0000313|EMBL:KQS56491.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS56491.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS56491.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS56491.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS56491.1}.
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DR EMBL; LMPZ01000002; KQS56491.1; -; Genomic_DNA.
DR RefSeq; WP_056103001.1; NZ_LMPZ01000002.1.
DR AlphaFoldDB; A0A0Q5VFW7; -.
DR STRING; 1736353.ASG17_03140; -.
DR OrthoDB; 9808822at2; -.
DR Proteomes; UP000051182; 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:UP000051182}.
FT DOMAIN 262..356
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 220..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 39379 MW; D7E7FB8BA01F789B CRC64;
MTDKIPVTVL TGYLGAGKTT LLNRILTEDH GKRYAVIVNE FGEIGIDNDL VVGADEDVFE
MNNGCVCCTV RGDLIRVVAG LMKRQRPGKP AFDAIIVETT GLADPGPVAQ TFFVDEEVKA
KTQLDSVTAL VDAKHVMARL DDSKEAREQV AFADRIILNK VDLASAEELD AVEARLRALN
PLAPIVRAER SNVPLDQVLG VHAFDLDRIL EVRPDWVNPP HGAEGHVHGD DCGHDHHDHD
HGHDHHHDHD HGPRGHAHQD DIKGVALSLD RPINGDKFTA WLDRLLAEQG QNILRAKGII
DLKGEDRRLV FQAVHMILEG DLQRPWGEAE RRWSRAVFIG RDLDEAALKA GFEACAA
//
