HISZ_THEMA
ID HISZ_THEMA Reviewed; 275 AA.
AC Q9X0D3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN Name=hisZ; OrderedLocusNames=TM_1043;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC allow the feedback regulation of ATP phosphoribosyltransferase activity
CC by histidine (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000305}.
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DR EMBL; AE000512; AAD36120.1; -; Genomic_DNA.
DR PIR; B72305; B72305.
DR RefSeq; NP_228849.1; NC_000853.1.
DR PDB; 1USY; X-ray; 2.52 A; A/B/C/D=1-275.
DR PDBsum; 1USY; -.
DR AlphaFoldDB; Q9X0D3; -.
DR SMR; Q9X0D3; -.
DR STRING; 243274.THEMA_09145; -.
DR EnsemblBacteria; AAD36120; AAD36120; TM_1043.
DR KEGG; tma:TM1043; -.
DR PATRIC; fig|243274.18.peg.1772; -.
DR eggNOG; COG3705; Bacteria.
DR InParanoid; Q9X0D3; -.
DR OMA; WYADFVY; -.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; Q9X0D3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..275
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171072"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 86..99
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 103..120
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1USY"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:1USY"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 261..274
FT /evidence="ECO:0007829|PDB:1USY"
SQ SEQUENCE 275 AA; 31289 MW; CFE7716DF9177EC1 CRC64;
MDFLDFEKVF SFYSKATKKG FSPFFVPALE KAEEPAGNFF LDRKGNLFSI REDFTKTVLN
HRKRYSPDSQ IKVWYADFVY RYSGSDLVAE YQLGLEKVPR NSLDDSLEVL EIIVESASEF
FEGPVIVEIG HTGVYEDLLK EIPKDLHEKV LNLIDTKNLA EIEFLSHMKK IDLSRVEKII
EDSIYRRSPE HLKTMDLPLS VREDLLSASS FLQEKFPTVS VEIDLTLART IEEYCGLIFT
IYDTSSSRLV AAGGEYTVNG EKGVGGSIFL EGKTC
