HISZ_ACIB5
ID HISZ_ACIB5 Reviewed; 388 AA.
AC B7IAF3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=AB57_1314;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001182; ACJ40336.1; -; Genomic_DNA.
DR RefSeq; WP_000155680.1; NC_011586.2.
DR AlphaFoldDB; B7IAF3; -.
DR SMR; B7IAF3; -.
DR KEGG; abn:AB57_1314; -.
DR HOGENOM; CLU_025113_0_1_6; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000007094; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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 PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT CHAIN 1..388
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000117668"
SQ SEQUENCE 388 AA; 42861 MW; F040D8CC75DE4426 CRC64;
MTISETWLLP DGVADVLPEQ AQVIEKLRRE AIDFLAVRGY QLVYTPFIEY IESLSSLSES
NQDLDLVTFK VIDQLSGRLL GIRADMTPQV ARIDAHVRPV EGVARYCYAG TVLHTKPQNF
NATRAPLQLG AELYGHDSIE ADVEMVDVML GLIENAYTLQ GAHLDLGHVG LFRSLVKYAG
LSKNEEHELS DLYQRKALPE LAEFTQNLNM GSDFYALGRY ASDLDALQAH LSADILKDAE
FDAALNALKT TLEQIKNRWP ALNVGIDVVE LRSYHYHTGL MYAVYAPNRA APLAQGGRYD
GIGEHFGRAR PATGFSCDLY ALGANQFAEI ETVVAPKGTE ADLLKAIANA RSEGLRVVQL
LGNDDLSSIP YATHQLVLQN GQWNIEKI