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Database: UniProt
Entry: B4VI79_9CYAN
LinkDB: B4VI79_9CYAN
Original site: B4VI79_9CYAN 
ID   B4VI79_9CYAN            Unreviewed;       235 AA.
AC   B4VI79;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisIE {ECO:0000256|HAMAP-Rule:MF_01019};
DE   Includes:
DE     RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01019};
DE              Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01019};
DE              EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01019};
DE   Includes:
DE     RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01019};
DE              Short=PRA-PH {ECO:0000256|HAMAP-Rule:MF_01019};
DE              EC=3.6.1.31 {ECO:0000256|HAMAP-Rule:MF_01019};
GN   Name=hisI {ECO:0000256|HAMAP-Rule:MF_01019};
GN   Synonyms=hisIE {ECO:0000256|HAMAP-Rule:MF_01019};
GN   ORFNames=MC7420_7028 {ECO:0000313|EMBL:EDX78375.1};
OS   Coleofasciculus chthonoplastes PCC 7420.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Coleofasciculus.
OX   NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX78375.1, ECO:0000313|Proteomes:UP000003835};
RN   [1] {ECO:0000313|EMBL:EDX78375.1, ECO:0000313|Proteomes:UP000003835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX78375.1,
RC   ECO:0000313|Proteomes:UP000003835};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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_01019};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC         ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001460, ECO:0000256|HAMAP-
CC         Rule:MF_01019};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000256|ARBA:ARBA00005204, ECO:0000256|HAMAP-Rule:MF_01019}.
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_01019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01019}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC       {ECO:0000256|ARBA:ARBA00007731, ECO:0000256|HAMAP-Rule:MF_01019}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC       {ECO:0000256|ARBA:ARBA00008299, ECO:0000256|HAMAP-Rule:MF_01019}.
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DR   EMBL; DS989841; EDX78375.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4VI79; -.
DR   STRING; 118168.MC7420_7028; -.
DR   eggNOG; COG0139; Bacteria.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_048577_3_1_3; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000003835; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 1.
DR   HAMAP; MF_01020; HisE; 1.
DR   HAMAP; MF_01021; HisI; 1.
DR   HAMAP; MF_01019; HisIE; 1.
DR   InterPro; IPR023019; His_synth_HisIE.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR026660; PRA-CH.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR   NCBIfam; TIGR03188; histidine_hisI; 1.
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   Pfam; PF01503; PRA-PH; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 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_01019};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01019};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01019};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01019};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01019};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01019};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01019}; Reference proteome {ECO:0000313|Proteomes:UP000003835}.
FT   DOMAIN          59..133
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF01502"
FT   REGION          1..146
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01019"
FT   REGION          147..235
FT                   /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01019"
SQ   SEQUENCE   235 AA;  26570 MW;  0800D1473378DDE4 CRC64;
     MFLANTGKLV IIARFRYCIM SSTVSSTSSQ AIPVEKIRYN DQGLVPAIVQ DYLDGTVLMM
     AWMNRESLQK TLDTGETWFW SRSRQELWHK GATSGHLQHV RSLRYDCDSD TLLIGVEQVG
     DIACHTGERS CFHQVDGIKA APPADTLSQV FEVICDRRDN PTPESYTCKL FKGGDNKILK
     KIGEEAAEVV MACKDDEKDA IASEAADLFY HTLVALAHHQ VDVRDVYRKL QERRR
//
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