HISZ_LISMF
ID HISZ_LISMF Reviewed; 392 AA.
AC Q722Y1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125};
GN OrderedLocusNames=LMOf2365_0598;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT03380.1; -; Genomic_DNA.
DR RefSeq; WP_010958765.1; NC_002973.6.
DR AlphaFoldDB; Q722Y1; -.
DR SMR; Q722Y1; -.
DR KEGG; lmf:LMOf2365_0598; -.
DR HOGENOM; CLU_025113_0_0_9; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; ISS:JCVI.
DR GO; GO:0030234; F:enzyme regulator activity; ISS:JCVI.
DR GO; GO:0000105; P:histidine biosynthetic process; ISS:JCVI.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00125; HisZ; 1.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT CHAIN 1..392
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171043"
SQ SEQUENCE 392 AA; 43868 MW; 13B0F808E64E4065 CRC64;
MNLNKNLPTG TRDKLFREAQ AAYKIEQQVN HYFEKRGFKR IETPVIEFED VFSSEHQADA
KLYRFFDEKG RLTVLRPDMT LPIGRVVSTT GVMLPLKLSY SGKIFRANED FGGEQNEQTQ
AGIEIIGYPS IKAEIECILS GIGVLNALEI PNFQIELGHA AIYRRVIQLL NLSETAEIDF
RQLIQNKSLT GIKRFVANNP STLDDFILAI PRLFGPATAI LNQAKSLTTD KGILTALREM
ETIVEAVSYT ADISVDLGLV QDFHYYTGII FRGYADLAAD NFLSGGRYDH LLEQFTSSSS
PAVGLALNLD SLTTLQNRAG IIKKQTPTTL LIHYDLEALP QAEKFMQETP NSELSFFETA
SNAISFAKKW HIPEVVHVSS QGIQTILQRE VD