ID B1Y6R0_LEPCP Unreviewed; 343 AA.
AC B1Y6R0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Cobalamin synthesis protein P47K {ECO:0000313|EMBL:ACB36088.1};
GN OrderedLocusNames=Lcho_3834 {ECO:0000313|EMBL:ACB36088.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB36088.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB36088.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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}.
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DR EMBL; CP001013; ACB36088.1; -; Genomic_DNA.
DR RefSeq; WP_012348835.1; NC_010524.1.
DR AlphaFoldDB; B1Y6R0; -.
DR STRING; 395495.Lcho_3834; -.
DR KEGG; lch:Lcho_3834; -.
DR eggNOG; COG0523; Bacteria.
DR HOGENOM; CLU_017452_0_2_4; -.
DR OrthoDB; 9808822at2; -.
DR Proteomes; UP000001693; Chromosome.
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:UP000001693}.
FT DOMAIN 248..342
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 224..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 38495 MW; 5C67796DC803AEE2 CRC64;
MSSGLIPATI LTGFLGSGKT TLLKRVLSEA HGQKIAVIEN EFGEENIDNE ILVADTKEQI
IQLSNGCICC SIREDLRSTL SDLATRRRKG ELDFDRVVIE TTGLADPGPV AQTFFMDDEV
AESYLLDSVL TLVDAKHAQK QLDDRQEARR QIGFADQLFI SKADLVDAAD LEALAHRLKH
MNPRAPQRPV NFGEVSIAEV FDLRGFNLNA KLEIDPEFLS ADEHAHDHHD HDHEHCDHPH
HHHHDDDVKS FVFRASRPFS PAKLEDFLGS VVQIYGPRML RYKGVLHMQG TDRKVIFQGV
HQLMGSDLGP KWEAAEERGS KMVFIGIDLP REVFQQGLEQ CLA
//
