HISZ_CELJU
ID HISZ_CELJU Reviewed; 396 AA.
AC B3PDB6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=CJA_3074;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE82797.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PDB6; -.
DR SMR; B3PDB6; -.
DR STRING; 498211.CJA_3074; -.
DR EnsemblBacteria; ACE82797; ACE82797; CJA_3074.
DR KEGG; cja:CJA_3074; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_6; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001036; 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; 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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..396
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000095454"
SQ SEQUENCE 396 AA; 43302 MW; D8B323F6A0FBEE64 CRC64;
MVRVVMTYAD RWLLPEGVEE ILPGEAKAID SLRRKLLDLY SAWGYDMVIP PLLEYTDSLL
TGSGRDIDLL TLKVTDQLSG RTLGIRADIT PQTARMDAHS FNRQGANRLC YAGHVVHARP
KNPLATRTPI QAGIEFYGEA DLAADIEVVS LLLESLQVAG LPRLHIDLGH VGIYRAIAND
AGLTTAQEQE FFELLQRKAV TEIHAWVEAN IPSADKAAAF ILLPSLAGGI EVLDRARSQF
AHLPQVIDAL DHLQQLAAVV MARYPSAELY FDLGEVRGYH YLTGIVFAAF APGYGNPIAS
GGRYDHIGEV FGRARPATGF AVDITALSKL GFIGQHDVSA IAVEVNQDPQ QWAAIKALRA
RGERVIQLTP AGQLAELKCD RQLLLLDGKY QVVPLQ