HISZ_NITOC
ID HISZ_NITOC Reviewed; 397 AA.
AC Q3J807;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Noc_2586;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA59039.1; -; Genomic_DNA.
DR RefSeq; WP_004269163.1; NC_007484.1.
DR AlphaFoldDB; Q3J807; -.
DR SMR; Q3J807; -.
DR STRING; 323261.Noc_2586; -.
DR EnsemblBacteria; ABA59039; ABA59039; Noc_2586.
DR KEGG; noc:Noc_2586; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_6; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000006838; 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 PIRSF; PIRSF001549; His-tRNA_synth; 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..397
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242843"
SQ SEQUENCE 397 AA; 44133 MW; 324BAF6BDE0F0B96 CRC64;
MPITERWLLP EGVGELLPIE AEQMERARRV LIDLFHSWGY DLVVPPLIEY LESLLTGVGT
DLELQTFKLT DQLTGRLMGV RADITPQVAR IAAHCIQRKG VTRLCYIGSV LHTLSQGLGG
TRNPIQVGAE LYGHSGTESD LEVLRLALEA LDVVGVKQVH LDLGHVGIFR DLVLQANLSP
EEEYGLFNIL QRKARDEIDT MLRNRDVGPQ LRHMFMALTS LNGGREVLDE AEQVLAGSGV
EQALTTLKEV ATLTDKYLPR VPMHFDLGEL RGYRYHTGLV FAAYIPGRGQ AVAQGGRYDD
IGQVFGRAQP ATGFSMDLKE LVTLGSSTTT TRLGIFAPWS EAPGFEREVA RLRQQGERVV
YGFPDTVSNY DELGCDRELV LKAKQWQIIE IRKLGRG