ID   HIS81_NITMU             Reviewed;         368 AA.
AC   Q2YAU6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase 1 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC1 {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=Nmul_A0818;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC         oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC         ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR   EMBL; CP000103; ABB74125.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2YAU6; -.
DR   SMR; Q2YAU6; -.
DR   STRING; 323848.Nmul_A0818; -.
DR   EnsemblBacteria; ABB74125; ABB74125; Nmul_A0818.
DR   KEGG; nmu:Nmul_A0818; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_4; -.
DR   OMA; IWLNANE; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000002718; Chromosome.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..368
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000230217"
FT   MOD_RES         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   368 AA;  40455 MW;  75B602836D70F64D CRC64;
     MAVMPFSPDQ IIRPEILALS AYHVPPACGM IKLDAMENPY PLPPELRDEI AKLAGETPVN
     RYPDPDAAAL KAALREALSI PDGMDIMLGN GSDEIIQIIA LACGKPGAVL MSVEPAFVMF
     RMIATFASMN YVGVPLHPDF SLDAEAMLAA IARYQPAVIF IAYPNNPTGN LFDAVEISRI
     IDAAPGVVVV DEAYHAFADA SFMDKLAHHP NLLLMRTLSK LGMAGLRLGL LAGKPEWLRQ
     LEKLRLPYNV GIVTQRIAEK LLQHRDVLLQ QAAAIKLERS SMSRRLAELE GIEVFPTDAN
     FILFRLNQDH KATQVFQELK QRGILVKNLD GAHPLLKNCL RVTVGMPDEN AQFLEVLQTL
     LVKVEAKA