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Database: UniProt
Entry: E3HP79_ACHXA
LinkDB: E3HP79_ACHXA
Original site: E3HP79_ACHXA 
ID   E3HP79_ACHXA            Unreviewed;       372 AA.
AC   E3HP79;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=CobW/HypB/UreG, nucleotide-binding domain protein 5 {ECO:0000313|EMBL:ADP19548.1};
GN   OrderedLocusNames=AXYL_06255 {ECO:0000313|EMBL:ADP19548.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP19548.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP19548.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP19548.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP19548.1; -; Genomic_DNA.
DR   RefSeq; WP_013396836.1; NC_014640.1.
DR   AlphaFoldDB; E3HP79; -.
DR   STRING; 762376.AXYL_06255; -.
DR   KEGG; axy:AXYL_06255; -.
DR   PATRIC; fig|762376.5.peg.6270; -.
DR   eggNOG; COG0523; Bacteria.
DR   HOGENOM; CLU_017452_0_0_4; -.
DR   OrthoDB; 9808822at2; -.
DR   Proteomes; UP000006876; 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}.
FT   DOMAIN          276..370
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
FT   REGION          232..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   372 AA;  41833 MW;  73CA632A237778AB CRC64;
     MNTPRSLDKM VPVTILTGFL GAGKTTLLKR ILTEYHGRRV AVIENEFGPE SIDNDLLVQD
     SNEEIIELSN GCVCCTVRGD LMRTLSELRA KREAGELNFE RVILETTGMA NPGPVCQTFF
     MDDDIAEYYR LDAVVTVVDA KHGMATLDAQ PEAQKQVGFA DRILISKRDL VNEVDYEALR
     HRLVHMNPRA PITPVNFGEV DLKSIIDISG FNLNSILDID PQFLADEHPD AAHDHVHDHD
     HGHDHGHDHD HDHEGDCGAH CNHAHHHHHH QHDDEIGAFV FRSNKPFDPA RLEEFLGGVV
     QVYGPDLMRY KGILYMKGIN RRMLFQGVHM MMGAEPGKPW TAAEKPSTKM VFIGRKLPQE
     IFTRGLEQCL AG
//
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