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Database: UniProt
Entry: E1X4Q5_HALMS
LinkDB: E1X4Q5_HALMS
Original site: E1X4Q5_HALMS 
ID   E1X4Q5_HALMS            Unreviewed;       450 AA.
AC   E1X4Q5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Cobalamin synthesis protein {ECO:0000313|EMBL:CBW27131.1};
GN   OrderedLocusNames=BMS_2332 {ECO:0000313|EMBL:CBW27131.1};
OS   Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS   (Bacteriovorax marinus).
OC   Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC   Halobacteriovoraceae; Halobacteriovorax.
OX   NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW27131.1, ECO:0000313|Proteomes:UP000008963};
RN   [1] {ECO:0000313|Proteomes:UP000008963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC   {ECO:0000313|Proteomes:UP000008963};
RX   PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA   Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA   Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA   Williams H.N., Stine O.C.;
RT   "A small predatory core genome in the divergent marine Bacteriovorax
RT   marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL   ISME J. 7:148-160(2013).
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; FQ312005; CBW27131.1; -; Genomic_DNA.
DR   RefSeq; WP_014244908.1; NC_016620.1.
DR   AlphaFoldDB; E1X4Q5; -.
DR   STRING; 862908.BMS_2332; -.
DR   KEGG; bmx:BMS_2332; -.
DR   PATRIC; fig|862908.3.peg.2220; -.
DR   eggNOG; COG0523; Bacteria.
DR   HOGENOM; CLU_017452_0_0_7; -.
DR   Proteomes; UP000008963; 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:UP000008963}.
FT   DOMAIN          355..448
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
SQ   SEQUENCE   450 AA;  50988 MW;  81E2A1FF998DB9C5 CRC64;
     MQELIPVTLV VGFLGSGKTT FINEILNGDH GKKIAVIENE FGEVGIDDEI LSGSNDLFVE
     MSNGCICCSI KGDLVESLNK LLVHAKNFEH IVIEATGMAN PGPIIETFFS SEELSRSFVL
     DSVIGLVDSE HFEKNLEKFE NSEEIAFYDQ IAFSETILLN KSDTRTSEEL TSIREKVKVK
     NPNAQIISTT HSKVDLSKVM GTRSFDLKAI EETMPSANAV EYPFSWAGVI ELKAGFYKFN
     IDHTHHNERM VFFKIDEDDL NDKIINYANS LFFSPQRRAK RGANVNVDEH ILLDFGGEHT
     GRNILDIEFD GNYAFFISDH PSHLQLKILN REENEIEFKT DHSFKKVEHF HGNEINSISL
     EFSGALNPQS FEMFLNVLYS QYRDEIYRSK GILHFYGNDS RVLFQGVYSS LKFDHGREWA
     DEQRINKIVF IGKGLIGPSL EAGLKNCIVE
//
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