ID A1ALD0_PELPD Unreviewed; 445 AA.
AC A1ALD0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000256|ARBA:ARBA00020397, ECO:0000256|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000256|HAMAP-Rule:MF_00125};
GN OrderedLocusNames=Ppro_0519 {ECO:0000313|EMBL:ABK98150.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98150.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK98150.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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:0000256|ARBA:ARBA00025246, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004667, ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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 {ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC HisZ subfamily. {ECO:0000256|ARBA:ARBA00005539, ECO:0000256|HAMAP-
CC Rule:MF_00125}.
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DR EMBL; CP000482; ABK98150.1; -; Genomic_DNA.
DR AlphaFoldDB; A1ALD0; -.
DR STRING; 338966.Ppro_0519; -.
DR KEGG; ppd:Ppro_0519; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_2_7; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 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 NCBIfam; TIGR00443; hisZ_biosyn_reg; 1.
DR PANTHER; PTHR43707:SF6; ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:ABK98150.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00125};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Ligase {ECO:0000313|EMBL:ABK98150.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732}.
FT DOMAIN 37..364
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 445 AA; 49542 MW; 383E121669D6E79D CRC64;
MLTFRDSNPM NNRLPDISLP FGVSDFLPDA AAKIGYIEDR IRRVFELWGF RRVITPKLEY
EDVMALGLGD GLKNKTYRFD DRQTGRLLAF PPDITPQIAR IVATRLAASP LPHRISYSGR
VLRQTESQTG RSREIFQSGV ELIGLDSPEA DAEMVAMAVE ALQGLGFSDF KIDLGQVEFF
RGIVESSGLS GQPLRDLLEA VARKDASAVA RICAESPLSE ESRREIASLP RLFGGREVVE
AADRVACNSR SRAALDNLRQ VLDILDIHGV SDYLTIDLGE TRGLDYHTGI TFEGFVTGLG
VPVCGGGRYD SLAGRYGFET PATGFTFDVL SLLQALERRP ELEASTARDF LLFNRGSDRR
QALETARLLR SRGYSTARDI IRRDVQPSLE YARRMNIRCM LVMGDESDKG VVRAIRTRDG
KTVRLASDML CRDGLMEYIE ENQGE
//
