ID Q0S573_RHOJR Unreviewed; 388 AA.
AC Q0S573;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Probable cobalamin synthesis protein {ECO:0000313|EMBL:ABG97313.1};
GN OrderedLocusNames=RHA1_ro05533 {ECO:0000313|EMBL:ABG97313.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97313.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG97313.1; -; Genomic_DNA.
DR RefSeq; WP_011597708.1; NC_008268.1.
DR AlphaFoldDB; Q0S573; -.
DR KEGG; rha:RHA1_ro05533; -.
DR PATRIC; fig|101510.16.peg.5577; -.
DR eggNOG; COG0523; Bacteria.
DR HOGENOM; CLU_017452_2_0_11; -.
DR OrthoDB; 9808822at2; -.
DR Proteomes; UP000008710; 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; PTHR43603; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1.
DR PANTHER; PTHR43603:SF1; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; CobW_C; 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:UP000008710}.
FT DOMAIN 268..359
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
SQ SEQUENCE 388 AA; 41612 MW; 3D59B45BF46CEC08 CRC64;
MTVTRPLPVT VLSGFLGAGK TTLLNHLLAN RDGRRVAVIV NDMSEVNIVP QALRAGGPPA
ALVAGQGHLD RTQEKLVELT NGCICCTLRE DLVEAVARLA KEGRFDHLVI ESTGISEPMP
VAATFDWEFE GGLSLGSVAA LDTMVTVVDA STFLGELAKG ERLDDRNLEA GEGDERSISD
LLVDQVEFAD VILLNKTDLV SESAAGAAEA TVRRLNPTAR LLRTARGVVD PGEVLGTGRY
NPEAAAELPG RAEELAGGHT PETEEYGIRS VTYRASRPFH PARLDQALGR FTGVLRSKGF
CWIASRPDLA AVWSQAGPNL VIEPAQLWAS ADETPGQEIV FIGVRLDPDG PRRILDPALL
TDDELASGSA AWVRFDDPLP AWEAVHRH
//
