ID I1XL22_METNJ Unreviewed; 396 AA.
AC I1XL22;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=Q7A_2281 {ECO:0000313|EMBL:AFI85091.1};
OS Methylophaga nitratireducenticrescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI85091.1, ECO:0000313|Proteomes:UP000009144};
RN [1] {ECO:0000313|EMBL:AFI85091.1, ECO:0000313|Proteomes:UP000009144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI85091.1,
RC ECO:0000313|Proteomes:UP000009144};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
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|ARBA:ARBA00011496, 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; CP003390; AFI85091.1; -; Genomic_DNA.
DR RefSeq; WP_014707459.1; NC_017857.3.
DR AlphaFoldDB; I1XL22; -.
DR STRING; 754476.Q7A_2281; -.
DR KEGG; mej:Q7A_2281; -.
DR PATRIC; fig|754476.3.peg.2254; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_6; -.
DR OrthoDB; 9769617at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000009144; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase 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; 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:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00125};
KW Glycosyltransferase {ECO:0000313|EMBL:AFI85091.1};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Transferase {ECO:0000313|EMBL:AFI85091.1}.
FT DOMAIN 12..325
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
SQ SEQUENCE 396 AA; 43837 MW; 1DC9EC9DBE104048 CRC64;
MTLKESWLLP EGIDELMPEE ATQLERMHRL LVDRMQSWGY HLVVPPLIEY LDSLLTGTAK
TLDLQTFKLI DQLSGRLLGV RADMTPQVAR IAAHRLRNNA EILRLCYIGS VLHTLPASQA
SSRNPIQLGA EIYGHAGPES DMESIQLMVE LLEISGATGS ISLDIGHVGI YRGLADYAEL
DQEQEQAIFS AMQRKALPEI LNLLSGYAIT ETARSMLAAL SELNGDVSVL DKAKQILHDA
PDSVLNALDT LVVLAEMAKQ RLPGIQLNFD LAELRGYHYH TGVVFAAYQS NSAQAIALGG
RYDDIGQDFG HAQPATGFSL DLKKLVTRFP KPTEKRQTIS TVWSMDPQQL EWVTNLREQG
NIVVFELPGS KTPSEKKLIQ QDGRWQVVET GTNTRG
//
