ID A9BXU9_DELAS Unreviewed; 349 AA.
AC A9BXU9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:ABX38375.1};
GN OrderedLocusNames=Daci_5747 {ECO:0000313|EMBL:ABX38375.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX38375.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX38375.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX38375.1; -; Genomic_DNA.
DR RefSeq; WP_012207544.1; NC_010002.1.
DR AlphaFoldDB; A9BXU9; -.
DR STRING; 398578.Daci_5747; -.
DR GeneID; 24117855; -.
DR KEGG; dac:Daci_5747; -.
DR eggNOG; COG0523; Bacteria.
DR HOGENOM; CLU_017452_1_0_4; -.
DR Proteomes; UP000000784; Chromosome.
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:UP000000784}.
FT DOMAIN 257..348
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
SQ SEQUENCE 349 AA; 38295 MW; 7A7FBD954B067D95 CRC64;
MQTAKIPATI VTGFLGSGKT TLLRHILDNA DGRRIAVIVN EFGELGIDGE ILKGCGIGCD
DEGNEREGAL YELANGCMCC TVQEEFFPVM RALAERRDQI DAVIIETSGL ALPKPLVQAF
QWPEIANVFT VDAVVTVVDT PAAASGQFAA NPQAVDELRR ADPNLDHESP LHELFEDQLG
AADLVVLNKT DLADAEALAR VTALVREELP PEVKIVQSSQ GRLPLDVVLG LAKAAETTID
QRVSHHDHDE DHDHDDFDSY VIDLPAVDRD RLLAALETLV EQHSILRVKG FADIPGKPMR
WLLQGVGRRF DHHFDRAWRE GEQRGTRLVF IGQDLDEAAL RKGLENVAA
//
