HISZ_AROAE
ID HISZ_AROAE Reviewed; 384 AA.
AC Q5P7C3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=AZOSEA06650;
GN ORFNames=ebA1250;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI06788.1; -; Genomic_DNA.
DR RefSeq; WP_011236516.1; NC_006513.1.
DR AlphaFoldDB; Q5P7C3; -.
DR SMR; Q5P7C3; -.
DR STRING; 76114.ebA1250; -.
DR EnsemblBacteria; CAI06788; CAI06788; ebA1250.
DR KEGG; eba:ebA1250; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_4; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000006552; 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..384
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242818"
SQ SEQUENCE 384 AA; 41427 MW; 4368472F533713AC CRC64;
MRWVLPDHIQ DALPAEADKI ERLRRRLLDA FRSHGYQLVV PPLLEYLDSL TTGAGQDLKL
RTFKLVDQLS GRTMGVRADM TPQVARIDAH LLNRRGVSRL CYCGSVLHTL PSTLTATREP
LQLGAELYGH AGLDADIEII RLLAEVMRLA EVPASRIDLG HVGLFRVLAA RAGMVPGREE
ELFDLLQAKD LPDLHALVAG VAEPVRSALL ALPGLYGGAE VLDKARVCLP DDAEIREALD
DLSRLAAALG DLPVSFDLAD LRGYHYHSGV VFAAYGGGSP AALALGGRYD RVGEAFGRGR
PATGFSLDLR ELAVRLADVG QPGAILAPAG GDAALEALVA QLRSRGEVVM TELPGHDGSW
NEAGCDRQLI RREGRWTVES LQGE