ID D4MZZ7_ANAHA Unreviewed; 120 AA.
AC D4MZZ7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021};
DE Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021};
DE EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021};
GN Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021};
GN ORFNames=CL2_12140 {ECO:0000313|EMBL:CBL38192.1}, DO83_13755
GN {ECO:0000313|EMBL:AQP40545.1}, ERS852425_02609
GN {ECO:0000313|EMBL:CUN09859.1}, ERS852475_00104
GN {ECO:0000313|EMBL:CUN43717.1}, ERS852520_01852
GN {ECO:0000313|EMBL:CUP64829.1}, ERS852571_02368
GN {ECO:0000313|EMBL:CUN07652.1};
OS Anaerostipes hadrus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38192.1, ECO:0000313|Proteomes:UP000008960};
RN [1] {ECO:0000313|EMBL:CBL38192.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38192.1,
RC ECO:0000313|Proteomes:UP000008960};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SSC/2.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL38192.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38192.1,
RC ECO:0000313|Proteomes:UP000008960};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000095553, ECO:0000313|Proteomes:UP000095564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUN09859.1,
RC ECO:0000313|Proteomes:UP000095598}, 2789STDY5834860
RC {ECO:0000313|EMBL:CUN43717.1, ECO:0000313|Proteomes:UP000095611},
RC 2789STDY5834908 {ECO:0000313|EMBL:CUP64829.1,
RC ECO:0000313|Proteomes:UP000095564}, and 2789STDY5834959
RC {ECO:0000313|EMBL:CUN07652.1, ECO:0000313|Proteomes:UP000095553};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AQP40545.1, ECO:0000313|Proteomes:UP000188159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPB5 {ECO:0000313|EMBL:AQP40545.1,
RC ECO:0000313|Proteomes:UP000188159};
RX PubMed=27264309; DOI=10.1038/srep27572;
RA Zhang Q., Wu Y., Wang J., Wu G., Long W., Xue Z., Wang L., Zhang X.,
RA Pang X., Zhao Y., Zhao L., Zhang C.;
RT "Accelerated dysbiosis of gut microbiota during aggravation of DSS-induced
RT colitis by a butyrate-producing bacterium.";
RL Sci. Rep. 6:27572-27572(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC phosphoribosyl-AMP. {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000024, ECO:0000256|HAMAP-
CC Rule:MF_01021};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01021};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01021};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01021};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00005169, ECO:0000256|HAMAP-Rule:MF_01021}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021}.
CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP-
CC Rule:MF_01021}.
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DR EMBL; CP012098; AQP40545.1; -; Genomic_DNA.
DR EMBL; FP929061; CBL38192.1; -; Genomic_DNA.
DR EMBL; CYXY01000015; CUN07652.1; -; Genomic_DNA.
DR EMBL; CYXT01000022; CUN09859.1; -; Genomic_DNA.
DR EMBL; CYZM01000001; CUN43717.1; -; Genomic_DNA.
DR EMBL; CZAU01000017; CUP64829.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MZZ7; -.
DR STRING; 649756.ERS852387_01886; -.
DR KEGG; bprl:CL2_12140; -.
DR PATRIC; fig|245018.3.peg.1531; -.
DR OrthoDB; 9795769at2; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000008960; Chromosome.
DR Proteomes; UP000095553; Unassembled WGS sequence.
DR Proteomes; UP000095564; Unassembled WGS sequence.
DR Proteomes; UP000095598; Unassembled WGS sequence.
DR Proteomes; UP000095611; Unassembled WGS sequence.
DR Proteomes; UP000188159; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 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 PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR SUPFAM; SSF141734; HisI-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01021};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01021};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01021};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01021};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01021};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01021}.
FT DOMAIN 39..112
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
SQ SEQUENCE 120 AA; 13849 MW; 950C376A3946F049 CRC64;
MSNEAKPLNS KMSFDEFKLN SDGMLTVVVQ DHKTNEVLMV AYMTKEAYDK TIETGIMTYY
SRSRDELWIK GETSGHYQYV KDLYIDCDRD TLLAKVKQIG AACHTGNYSC FYTDLLEKED
//
