HISZ_GEOSL
ID HISZ_GEOSL Reviewed; 438 AA.
AC P60837;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=GSU3307;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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; AE017180; AAR36697.1; -; Genomic_DNA.
DR RefSeq; NP_954347.1; NC_002939.5.
DR RefSeq; WP_010943919.1; NC_002939.5.
DR AlphaFoldDB; P60837; -.
DR SMR; P60837; -.
DR STRING; 243231.GSU3307; -.
DR EnsemblBacteria; AAR36697; AAR36697; GSU3307.
DR KEGG; gsu:GSU3307; -.
DR PATRIC; fig|243231.5.peg.3325; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_0_2_7; -.
DR InParanoid; P60837; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR036621; Anticodon-bd_dom_sf.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..438
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171035"
SQ SEQUENCE 438 AA; 48417 MW; 026F3422E65A6340 CRC64;
MTPITPIEAP LPKGVTDFLP EKADKIGYIE GKIRKVFELW GFRRIITPLL EFEDVIAAGL
GDDLKAKTFR FDDRQSGKLI AVPSDITPQI ARIVATRLRG YPLPHRICYS GRVLRHAELQ
SGRSREIFQS GVELIGLDSP EADAEMVTMA VEALKGLGFR DFKIDLGHVG FIRGIMTASG
LEVAVRNRLQ EAIGKKDVSA VRSILAESPL SDAAKDELAA LPRLFGGREV LDEAGRVATN
DTSRRALDNI SQVLDLLDIH GVSDHLTIDL GEVRGLDYHT GLTFEGFVTG MGEAVCSGGR
YDTLTARYGF PAPATGFTFN VLALLSALEK RPDVEASKTR DILIFNQQDD RREALEIAQQ
LRRRGYTTAR DIIRRNFDDS LDYARRMNIL HMMVVGGDQC GPDEVYLVRV ADGQGQRIKK
AEVFSERFSL DAGPDKES