ID A0A0L6JSU3_9FIRM Unreviewed; 419 AA.
AC A0A0L6JSU3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=Bccel_4039 {ECO:0000313|EMBL:KNY28765.1};
OS Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudobacteroides.
OX NCBI_TaxID=398512 {ECO:0000313|EMBL:KNY28765.1, ECO:0000313|Proteomes:UP000036923};
RN [1] {ECO:0000313|Proteomes:UP000036923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2933 {ECO:0000313|Proteomes:UP000036923};
RA Dassa B., Utturkar S.M., Klingeman D.M., Hurt R.A., Keller M., Xu J.,
RA Reddy Y.H.K., Borovok I., Grinberg I.R., Lamed R., Zhivin O., Bayer E.A.,
RA Brown S.D.;
RT "Near-Complete Genome Sequence of the Cellulolytic Bacterium Bacteroides
RT (Pseudobacteroides) cellulosolvens ATCC 35603.";
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNY28765.1}.
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DR EMBL; LGTC01000001; KNY28765.1; -; Genomic_DNA.
DR RefSeq; WP_036936281.1; NZ_LGTC01000001.1.
DR AlphaFoldDB; A0A0L6JSU3; -.
DR STRING; 398512.Bccel_4039; -.
DR PATRIC; fig|398512.5.peg.4223; -.
DR eggNOG; COG3705; Bacteria.
DR OrthoDB; 9800814at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000036923; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR036621; Anticodon-bd_dom_sf.
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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00125};
KW Glycosyltransferase {ECO:0000313|EMBL:KNY28765.1};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Ligase {ECO:0000313|EMBL:KNY28765.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036923};
KW Transferase {ECO:0000313|EMBL:KNY28765.1}.
FT DOMAIN 22..334
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 419 AA; 47172 MW; 082BF21006F5F3A1 CRC64;
MSKWKIYTPE GVQDILFNEC YLKRNLEVKL RSIFRSSGYQ EIETPTFEFY DVFSEDSDMT
PQENMFKFFD QQGRILVLRP EMTIPVARIS ATKCKDISVP VRYSYIGNTF NYNELGGGKQ
KEFTQAGIEM VGVNTPEADA EVIATAITAV KAMGLESFQI DIGQVEFFKG LMEEAGIADN
DIEQMRVLID RKDFLGVEEL VKGQDIKEDL KELIFSLPRL FGSIDVIEKV EKITLNKRSL
NALNNLRKVL QILDDYGYSK YVSVDLGMVR SLNYYTGIIF RGFTYGAGFP ILSGGRYDSL
VGKFGKSTPA IGFSLGVNMI MIALDRQKID TEKPKIDTLV CYMNEGRKAA FKVAQELRRQ
GLAVEIDVAC QGVEQLKGYA ASKKIGGIIL IKDDENIEIH NLETGEASKV TFAELIRHD
//
