ID R6MQZ4_9FIRM Unreviewed; 451 AA.
AC R6MQZ4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=BN647_01615 {ECO:0000313|EMBL:CDB96646.1};
OS Firmicutes bacterium CAG:41.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263021 {ECO:0000313|EMBL:CDB96646.1, ECO:0000313|Proteomes:UP000018139};
RN [1] {ECO:0000313|EMBL:CDB96646.1, ECO:0000313|Proteomes:UP000018139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:41 {ECO:0000313|Proteomes:UP000018139};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDB96646.1}.
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DR EMBL; CBEM010000093; CDB96646.1; -; Genomic_DNA.
DR AlphaFoldDB; R6MQZ4; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000018139; 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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 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; 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:CDB96646.1};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000018139};
KW Transferase {ECO:0000313|EMBL:CDB96646.1}.
FT DOMAIN 22..324
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 451 AA; 50564 MW; 4A41D3254BEF06F1 CRC64;
MSNWKLHTPN GVNDILPDEC AVKKEIESTI WSVFSSIGYK EVETPTFEYY DCYLGLSGQI
SQEHMFKFFD EQGRILALRP DFTTSIARMA ATKVANSDKP QRYLYTGNVY RVEQTQGARQ
REFTQSGIEL IGSYSPAADA EVISAAMEAV LAVGIEEFSM EIGQIAFFNG LVKQAGLDEQ
SIEKLRERID SKDSVGIKTI TDKLDIDDNI KNLMIDLPYL FGGEEVFKKA YVDGLNEESK
NALDNLKRIY ELLCLYGFEK YVSIDLGMLE SIDYYTGSIF KCYTHGVGFP ICAGGRYDNL
MGQFGDNKGA VGAAIGINRL ISVLSDKEVH DVSASLVFAE KNAEGIAYDI AYNLRVNGCL
VEMYIGDGDY KAAEEYSKGK NIGAMLRVFP NGQLMINDFA KHEIIETTAN EFLGYYDESM
MFDEHDHCGC GCDHDHEHEH HHDHCDCGHE H
//
