ID   HISZ_MARMS              Reviewed;         392 AA.
AC   A6VYL1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Mmwyl1_2627;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) 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; CP000749; ABR71540.1; -; Genomic_DNA.
DR   RefSeq; WP_012070316.1; NC_009654.1.
DR   AlphaFoldDB; A6VYL1; -.
DR   SMR; A6VYL1; -.
DR   STRING; 400668.Mmwyl1_2627; -.
DR   EnsemblBacteria; ABR71540; ABR71540; Mmwyl1_2627.
DR   KEGG; mmw:Mmwyl1_2627; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_1_6; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
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; 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_1000076246"
SQ   SEQUENCE   392 AA;  42886 MW;  DBD8653BA07E28A0 CRC64;
     MTLADRWLLP EGVDEALPEQ AAKIEHLRRT LLNLHESWGY HLVIPPLLEY LDSLLTGAGS
     DLEIETFKVI DQLSGRLLGI RADFTSQVAR IDAHCLKDDG VQRLSYCGSV LRTMPAGLDG
     TRSPIQLGAE IYGHGGVESD VEVLSLMLQT LSTAGLSNLV LDLGHVDIVS GVLAACNLNA
     DQESKLIELY KAKDLPELDR YAEELGCLTD IQKQWLVGLP RLCGGKEVLK HATDLLGDVN
     ESIRDAIVLL QKVSDSICQR FPKVGLHFDL SDLVSYSYHT GVIFAAYVPG HGNAIARGGR
     YNNIGQVFGR SRPATGFSTD VKALVALTDI VVNKPKTVLS PICSSDELWQ KANSLRAEGY
     RVVEVLDDIC AGDADFKLEF VDEAWQLMPV HN