ID A0A099GJ40_9RHOB Unreviewed; 336 AA.
AC A0A099GJ40;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:KGJ22173.1};
GN ORFNames=IX56_09635 {ECO:0000313|EMBL:KGJ22173.1};
OS Paracoccus sanguinis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ22173.1, ECO:0000313|Proteomes:UP000029858};
RN [1] {ECO:0000313|EMBL:KGJ22173.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22173.1,
RC ECO:0000313|Proteomes:UP000029858};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ22173.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22173.1,
RC ECO:0000313|Proteomes:UP000029858};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) 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:KGJ22173.1}.
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DR EMBL; JRKQ01000044; KGJ22173.1; -; Genomic_DNA.
DR RefSeq; WP_036709639.1; NZ_JRKQ01000044.1.
DR AlphaFoldDB; A0A099GJ40; -.
DR Proteomes; UP000029858; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
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; IPR012824; CobW.
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 NCBIfam; TIGR02475; CobW; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR PANTHER; PTHR13748:SF70; PROTEIN COBW; 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:UP000029858}.
FT DOMAIN 246..335
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
SQ SEQUENCE 336 AA; 35461 MW; 8303C8B38959E396 CRC64;
MPLEKTPVTI VTGFLGAGKT TLIRHLLQNP GGRRLAVLVN EFGDVGVDGD LIRACADADC
PEANILELTN GCICCTVADE FIPAIERLMA LDPRPDNIVI ETSGLALPKP LLKAFDWPEL
RSRITIDGVV AVADAEAVAA GMFAPDPAHT GTEADHETPL SEVFEDQIAC ADLVLLSKAD
LAGPEGLEAA RQIIAAEAPR AVPMLPLTDG VIDARVVLGI GAAVEDGIDA RPSHHDGEAD
HDHDDFDAVV IDLPEVDDPQ ALAAKVADLA AAQRILRVKG HVAVSGKPMR LLVQAVGARV
RHQFDRPWGA QPRQGRLVVI AEKGDLDADA VKAALI
//
