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Database: UniProt/SWISS-PROT
Entry: HIS3_AGRFC
LinkDB: HIS3_AGRFC
Original site: HIS3_AGRFC 
ID   HIS3_AGRFC              Reviewed;         150 AA.
AC   Q8UEK7;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 1.
DT   28-FEB-2018, entry version 87.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01021};
DE            Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01021};
DE            EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01021};
GN   Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021};
GN   OrderedLocusNames=Atu1750; ORFNames=AGR_C_3213;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium
OS   tumefaciens (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
RA   Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
RA   Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
RA   Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
RA   Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
RA   Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
RA   Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
RA   Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
RA   Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
RA   Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA   Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA   Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA   Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA   Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA   Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1-
CC       (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-
CC       ribosylamino)methylideneamino)imidazole-4-carboxamide.
CC       {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01021};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01021};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01021};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01021};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01021}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000255|HAMAP-
CC       Rule:MF_01021}.
DR   EMBL; AE007869; AAK87520.2; -; Genomic_DNA.
DR   PIR; AG2791; AG2791.
DR   PIR; G97570; G97570.
DR   RefSeq; NP_354735.2; NC_003062.2.
DR   RefSeq; WP_010971841.1; NC_003062.2.
DR   ProteinModelPortal; Q8UEK7; -.
DR   SMR; Q8UEK7; -.
DR   STRING; 176299.Atu1750; -.
DR   EnsemblBacteria; AAK87520; AAK87520; Atu1750.
DR   GeneID; 1133788; -.
DR   KEGG; atu:Atu1750; -.
DR   PATRIC; fig|176299.10.peg.1763; -.
DR   eggNOG; ENOG4105K8F; Bacteria.
DR   eggNOG; COG0139; LUCA.
DR   HOGENOM; HOG000277504; -.
DR   KO; K01496; -.
DR   OMA; TGYRSCF; -.
DR   BioCyc; AGRO:ATU1750-MONOMER; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000000813; Chromosome circular.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.20.400; -; 1.
DR   HAMAP; MF_01021; HisI; 1.
DR   InterPro; IPR026660; PRA-CH.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR   Pfam; PF01502; PRA-CH; 1.
DR   ProDom; PD002610; PRA_CycHdrlase; 1.
DR   SUPFAM; SSF141734; SSF141734; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN         1    150       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_0000136456.
FT   METAL        92     92       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        93     93       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL        94     94       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL        96     96       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01021}.
FT   METAL       111    111       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
FT   METAL       118    118       Zinc; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01021}.
SQ   SEQUENCE   150 AA;  16483 MW;  A70554EE4F2799ED CRC64;
     MSIPFPSAPA DKEALENAGL FSPKFDAHGL VTAVVTDARD GELLMVAHMN AEALSLTLET
     GIAHYYSRSR DKIWKKGETS GNLQTVKEFR TDCDQDAVWL KVSVAGHDAT CHTGRRSCFY
     RTVELSNGDA VTKITDDTRH FDPATTYSNT
//
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