HISZ_NOSP7
ID HISZ_NOSP7 Reviewed; 403 AA.
AC B2IWE2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Npun_F1161;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC allow the feedback regulation of ATP phosphoribosyltransferase activity
CC by histidine. {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00125}.
CC -!- MISCELLANEOUS: This function is generally fulfilled by the C-terminal
CC part of HisG, which is missing in some bacteria such as this one.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC HisZ subfamily. {ECO:0000255|HAMAP-Rule:MF_00125}.
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DR EMBL; CP001037; ACC79887.1; -; Genomic_DNA.
DR RefSeq; WP_012407908.1; NC_010628.1.
DR AlphaFoldDB; B2IWE2; -.
DR SMR; B2IWE2; -.
DR STRING; 63737.Npun_F1161; -.
DR EnsemblBacteria; ACC79887; ACC79887; Npun_F1161.
DR KEGG; npu:Npun_F1161; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_2_3; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR PhylomeDB; B2IWE2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001191; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00125; HisZ; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR004517; HisZ.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..403
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000095463"
SQ SEQUENCE 403 AA; 45349 MW; 4F37BBD5649C9F4E CRC64;
MVYQPASGAR DLLPLDVEKK RWIEDRLQQV FHRWGYHRII TSTLERMDTL MAGEAIQRQM
VIQLQNGEDD ELGLRPELTA SIARTVVTRM ANATYPQRLY YNANVFRRTW ESRHNRQQEF
YQAGVELLGA GGLLANAEVL LLVADCLAAL GLRQWHLILG EAGITRSLLS AFPANLQDKV
RSAIAHLDRI TIDTLPLSDK LRDRAQIIMD LRGPSADVLQ KVSSLDLDEE QREAVNNLKS
LVELLESEKK FPLILDLSLI QTIDYYTGIV FEVVNDTESQ ARVLGRGGRY DQLLGLYHPQ
RENIPGIGFG LSIEDLYQVL LSTQQLPQVT PASNYLVVPE TGSANAAAFA YAQKLRDSTD
LVRVEIDLGG RDAEAIRQYA RDRSIAQIAW IKADSSPKIE SLR