ID A0A0Q6Z5A6_9BRAD Unreviewed; 351 AA.
AC A0A0Q6Z5A6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:KQW18884.1};
GN ORFNames=ASC80_15395 {ECO:0000313|EMBL:KQW18884.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW18884.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW18884.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18884.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW18884.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18884.1,
RC ECO:0000313|Proteomes:UP000051348};
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:KQW18884.1}.
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DR EMBL; LMDP01000003; KQW18884.1; -; Genomic_DNA.
DR RefSeq; WP_056299161.1; NZ_LMDP01000003.1.
DR AlphaFoldDB; A0A0Q6Z5A6; -.
DR STRING; 1736436.ASC80_15395; -.
DR OrthoDB; 9808822at2; -.
DR Proteomes; UP000051348; 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:UP000051348}.
FT DOMAIN 255..349
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 219..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 39419 MW; D49E9858499E1298 CRC64;
MSDVAANKIP VTVLTGYLGA GKTTLLNRIL SENHGKKYAV IVNEFGEIGI DNDLIIGADE
EVFEMNNGCV CCTVRGDLVR ILDGLMKRKG KFDAIILETT GLADPAPVAQ TFFVDEDVRE
KTALDAVVTV ADAKWLSSRL KDAPEAKNQI AFADVIVLNK TDLVSKPELA EVEARIRAIN
PYATLHRTER CQVQLSDVLG RGAFDLDRIL EIEPGFLEDD SHDHDHGHDH HHDGHDHHHH
DHAHHGMKHY HDEDMQSLSL HSDKPLDPTK FMPWLQQLVA EDGMNILRSK GILAFQGDDD
RYVFQGVHMM LEGDHQRKWK DDEARVSRLV FIGRELPEQK IRDGFAKCIV A
//
