HISZ_PSYA2
ID HISZ_PSYA2 Reviewed; 387 AA.
AC Q4FTX3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Psyc_0676;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAZ18535.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000082; AAZ18535.1; ALT_INIT; Genomic_DNA.
DR PDB; 5M8H; X-ray; 2.34 A; A/B/C/D=1-387.
DR PDB; 6FTT; X-ray; 2.29 A; A/B/C/D=1-387.
DR PDB; 6FU2; X-ray; 2.71 A; A/B=1-387.
DR PDB; 6FU7; X-ray; 2.31 A; A/B=1-387.
DR PDB; 6FUA; X-ray; 2.80 A; A/B=1-387.
DR PDB; 6R02; X-ray; 2.65 A; A/B/C/D=1-387.
DR PDB; 7Z6R; X-ray; 2.55 A; A/B=1-387.
DR PDBsum; 5M8H; -.
DR PDBsum; 6FTT; -.
DR PDBsum; 6FU2; -.
DR PDBsum; 6FU7; -.
DR PDBsum; 6FUA; -.
DR PDBsum; 6R02; -.
DR PDBsum; 7Z6R; -.
DR AlphaFoldDB; Q4FTX3; -.
DR SMR; Q4FTX3; -.
DR STRING; 259536.Psyc_0676; -.
DR EnsemblBacteria; AAZ18535; AAZ18535; Psyc_0676.
DR KEGG; par:Psyc_0676; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_6; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000546; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..387
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242851"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6FTT"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6FTT"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6FTT"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:6FTT"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:6FTT"
FT HELIX 338..354
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:6FTT"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:6FTT"
SQ SEQUENCE 387 AA; 43028 MW; A89339C74762F34B CRC64;
MLPDGVADVL FEDAHKQEVL RHQLTQQLIT HGYQLVSPPM IEFTESLLSG ASEDLKRQTF
KIIDQLTGRL MGIRADITPQ ILRIDAHHGG DGIARYCYAG DVIHTLPSGL FGSRTPLQLG
AEIFGCESIA ADIELIDVLF SMINSLDMSA VLHVDLGHVT IFKRLAELAA LSASDTEQLM
QLYANKNLPE LKQVCQVLPM GSDFYTLARF GHDIANLLGR LSENAQQDTK IVTAIDELQR
LKAHLQVQWQ CAVSIDVTEL SGYHYHTGIV FNGYINSETQ PLVRGGRFDG MKSNQLATNQ
PRQATGFSMD VSRLLAHTQL DAPFIVLIDY DAFNNLDSAQ RQLLLQQVAS LRQQGYRVTM
PLTAEDMPVG LTHRLSLADN QWRLHAV
