HIS2_SCHPO
ID HIS2_SCHPO Reviewed; 417 AA.
AC O59667;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Histidine biosynthesis bifunctional protein his7 {ECO:0000250|UniProtKB:P00815, ECO:0000312|EMBL:CAA18379.1};
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000250|UniProtKB:P00815};
DE EC=3.5.4.19;
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000250|UniProtKB:P00815};
DE EC=3.6.1.31;
GN Name=his7 {ECO:0000312|EMBL:CAA18379.1}; ORFNames=SPBC29A3.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA18379.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000250|UniProtKB:P00815}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000250|UniProtKB:P00815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- CAUTION: In contrast to other fungi which have a single histidine
CC biosynthesis trifunctional protein, 2 proteins are present in S.pombe
CC to ensure these functions: his7 (phosphoribosyl-AMP cyclohydrolase and
CC phosphoribosyl-ATP pyrophosphatase activities) and his2 (histidinol
CC dehydrogenase activity). {ECO:0000305}.
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DR EMBL; CU329671; CAA18379.1; -; Genomic_DNA.
DR PIR; T40073; T40073.
DR RefSeq; NP_595830.1; NM_001021734.2.
DR AlphaFoldDB; O59667; -.
DR SMR; O59667; -.
DR BioGRID; 276821; 22.
DR STRING; 4896.SPBC29A3.02c.1; -.
DR iPTMnet; O59667; -.
DR MaxQB; O59667; -.
DR PaxDb; O59667; -.
DR PRIDE; O59667; -.
DR EnsemblFungi; SPBC29A3.02c.1; SPBC29A3.02c.1:pep; SPBC29A3.02c.
DR GeneID; 2540290; -.
DR KEGG; spo:SPBC29A3.02c; -.
DR PomBase; SPBC29A3.02c; his7.
DR VEuPathDB; FungiDB:SPBC29A3.02c; -.
DR eggNOG; KOG4311; Eukaryota.
DR HOGENOM; CLU_041225_0_0_1; -.
DR InParanoid; O59667; -.
DR OMA; QTGKGFC; -.
DR PhylomeDB; O59667; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR PRO; PR:O59667; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IGI:PomBase.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; ISO:PomBase.
DR GO; GO:0000105; P:histidine biosynthetic process; IGI:PomBase.
DR Gene3D; 3.10.20.810; -; 1.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR012131; Hstdl_DH.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF141734; SSF141734; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Multifunctional enzyme; Nucleotide-binding; Reference proteome.
FT CHAIN 1..417
FT /note="Histidine biosynthesis bifunctional protein his7"
FT /id="PRO_0000352786"
FT REGION 225..299
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000255"
FT REGION 303..387
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 417 AA; 46183 MW; F3911725940AFD74 CRC64;
MALLPFFDLT NFESDASEEL GWLKYVGRVQ TRVFPQHFKD NLEKVRKISE TIDVIVDTTA
ELGPEACVNL LNAGALAILV NEEMLNELAD ISPNRLVLKT DTTDIGKIEK LSQVAGSIQW
IGSAENYPPD FFERASKIIH KAVMPEGGGR TLYLEFPEQP SMEVLKSFSV HSVVPVLSSS
FLTVKPAEEP KKLSLADLIL ISANTDREDG LFSTLVVNEL GIALGLVYSS KESVAESLKT
GTGVYQSRKR GLWYKGASSG AVQHLIHIDV DCDEDCLRFV VYQTGKGFCH LDTLHCFGQA
SGLCQLEKTL IDRKNNAPEG SYTARLFSDP KLLRAKIMEE AEELCDATTK ENVIWEMADL
MYFAITRCVG SGVSLNDISR HLDLKHRKVT RRKGDAKVAW QEKLKDKGGV ANTSYTA
