HISZ_ALKHC
ID HISZ_ALKHC Reviewed; 397 AA.
AC Q9K6Z0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=BH3584;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB07303.1; -; Genomic_DNA.
DR PIR; H84097; H84097.
DR PDB; 3OD1; X-ray; 1.97 A; A/B=1-397.
DR PDBsum; 3OD1; -.
DR AlphaFoldDB; Q9K6Z0; -.
DR SMR; Q9K6Z0; -.
DR STRING; 272558.10176208; -.
DR DNASU; 893798; -.
DR EnsemblBacteria; BAB07303; BAB07303; BAB07303.
DR KEGG; bha:BH3584; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_0_9; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; Q9K6Z0; -.
DR Proteomes; UP000001258; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..397
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171025"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3OD1"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 237..255
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:3OD1"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3OD1"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:3OD1"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3OD1"
SQ SEQUENCE 397 AA; 44254 MW; 28DFEFBB9E0141F7 CRC64;
MSKPFMFEKP FGMRDTLPEW YKTKKNICDQ MTEEINLWGY DMIETPTLEY YETVGVVSAI
LDQQLFKLLD QQGNTLVLRP DMTAPIARLV ASSLKDRAYP LRLAYQSNVY RAQQNEGGKP
AEFEQLGVEL IGDGTASADG EVIALMIAAL KRAGLSEFKV AIGHVGYVNA LLMDVVGNEQ
RADRLRRFLY EKNYVGYREH VKSLNLSTID KSRLMNLLSL RGGRAAIEEA RGLIQTEKGK
TALAEMTKLY EVLESYGASE YVKFDLTLVL HMSYYTGVVF EGYGNRLGVP LCSGGRYDEL
LSKFHRPAQA TGFGVRIDLL VEALNGEIIS NGHEQTCILF SNERRFEAIE LARKKRANGE
AVVLQDLAGV TDVDAMSSNY QDVIYCIGTA GRGGEDA
