HIS3_METCA
ID HIS3_METCA Reviewed; 128 AA.
AC Q603K4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=MCA2801;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000255|HAMAP-
CC 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-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-Rule:MF_01021};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC 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}.
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DR EMBL; AE017282; AAU91080.1; -; Genomic_DNA.
DR RefSeq; WP_010962002.1; NC_002977.6.
DR AlphaFoldDB; Q603K4; -.
DR SMR; Q603K4; -.
DR STRING; 243233.MCA2801; -.
DR EnsemblBacteria; AAU91080; AAU91080; MCA2801.
DR KEGG; mca:MCA2801; -.
DR eggNOG; COG0139; Bacteria.
DR HOGENOM; CLU_048577_5_0_6; -.
DR OMA; TGYRSCF; -.
DR OrthoDB; 1842189at2; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; ISS:JCVI.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; ISS:JCVI.
DR Gene3D; 3.10.20.810; -; 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 SUPFAM; SSF141734; SSF141734; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW Magnesium; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..128
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /id="PRO_0000229825"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
SQ SEQUENCE 128 AA; 14405 MW; ECA01DDC7A0AB394 CRC64;
MSAWLDEIRW TADGLVPVVA QEAGTGQVLM VAWMNREALA LTAAEGYAVY WSRSRGRLWR
KGEESGHRQK VLEIRIDCDE DVVLLKVEQA GGIACHTGRH HCFYRVLQDG RWVTVEPVLK
PPDSIYGA
