HISZ_SYNE7
ID HISZ_SYNE7 Reviewed; 420 AA.
AC Q55267; Q31Q24;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN Name=hisZ; OrderedLocusNames=Synpcc7942_0813;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7961432; DOI=10.1128/jb.176.21.6764-6768.1994;
RA Tsinoremas N.F., Kutach A.K., Strayer C.A., Golden S.S.;
RT "Efficient gene transfer in Synechococcus sp. strains PCC 7942 and PCC 6301
RT by interspecies conjugation and chromosomal recombination.";
RL J. Bacteriol. 176:6764-6768(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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 (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000305}.
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DR EMBL; L35476; AAA64445.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB56845.1; -; Genomic_DNA.
DR RefSeq; WP_011243038.1; NC_007604.1.
DR AlphaFoldDB; Q55267; -.
DR SMR; Q55267; -.
DR STRING; 1140.Synpcc7942_0813; -.
DR PRIDE; Q55267; -.
DR EnsemblBacteria; ABB56845; ABB56845; Synpcc7942_0813.
DR KEGG; syf:Synpcc7942_0813; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_2_3; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0813-MON; -.
DR BRENDA; 6.1.1.21; 6187.
DR UniPathway; UPA00031; UER00006.
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.
FT CHAIN 1..420
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171069"
FT CONFLICT 192
FT /note="L -> F (in Ref. 1; AAA64445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46534 MW; 175CC48D4BFD01CD CRC64;
MVHQPPAGTR DLLPQDVTQK RWIESRLQQV FQQWGYQRII TPTLERLDTL VAGGAVQRSA
VIQVQSDEES GLGLRPELTA SIARAAVTRL AGSSLPLRLY YLANVFRPAF QGDRLQQREL
FQAGVELLGV GGTLADAEVL HVLADALAEL GFGQPPLGSW HLVVGEASLT RSLLQPFPKD
LREKVRQAIA QLDRVTLESL PLESQLRDRA LLLHDLRGQP DQVFAKLQQL TLTPLEQTLR
DRLAQLVELY NASAGPQDSP LLLDLSLLRS FDYYTGIVFE VVYETPTGPW VLAQGGRYDR
LLDVYDPQAA GQPGIGFSCN IENLQQVLLA ANRLPHRPPA IDQLVIPVDS EAYGAALAEA
QRLQRQDQLR VELYLDSDRR PEVVQAFAQR RRIGRIVWVS SGSAPQSEAV AVAERATTTC