HISZ_SYNJB
ID HISZ_SYNJB Reviewed; 434 AA.
AC Q2JMG5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=CYB_1100;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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; CP000240; ABD02076.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2JMG5; -.
DR SMR; Q2JMG5; -.
DR STRING; 321332.CYB_1100; -.
DR KEGG; cyb:CYB_1100; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_2_3; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001938; 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..434
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242864"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 47515 MW; 1E4B74F9DD13A990 CRC64;
MYGRGSGAEH SRGSGAEHFW DPRPEASSTV SSSLRPPSGA RDLLPREVQR REKLEAQLTR
VFRRHGYQRI ITPTLERLET LLAGGSIRAE SVLQLRDGEG TMLGLRPEFT ASIVRAAATR
LAGGPLPLRL YYHGSVFRNS RREEGSYSSQ EFFQSGVELI GAGGWLADAE ILLLLADCIR
SVGISSCEFS WTLLLGDVSL TESLLSAVAP TAQAAVRRAI AQLDYVYLES APLPEAARQI
GLQILGLRGQ PGSVLSDLAQ LPVPPERLRD LRQLCQVLEE HGVRVVLDLS LLQTLAYYTG
IVFQAVASGE IIALGGRYDR LYALYSPQQV EQPGIGFTLL PDTLLRLLPP DPQTEEMGCK
RLVVPLVPAG IPAALALAAR WREECTAPLT RTEAVELELL DRAPEEIEAY ARQCRIPEIA
WVQADGSYHI THPG