HIS81_IDILO
ID HIS81_IDILO Reviewed; 367 AA.
AC Q5QZ49;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=IL1358;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV82198.1; -; Genomic_DNA.
DR RefSeq; WP_011234604.1; NC_006512.1.
DR AlphaFoldDB; Q5QZ49; -.
DR SMR; Q5QZ49; -.
DR STRING; 283942.IL1358; -.
DR EnsemblBacteria; AAV82198; AAV82198; IL1358.
DR KEGG; ilo:IL1358; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_6; -.
DR OMA; NYHVAGF; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001171; 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Histidinol-phosphate aminotransferase 1"
FT /id="PRO_0000153373"
FT MOD_RES 229
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 367 AA; 40505 MW; A7B889BCCE38CEC1 CRC64;
MAEFNALELV NPGVKQLRPY QAGKPTSELQ RELGLQHVVK LASNENPLGL SEKVKTALEA
ELTDLVRYPD ANGYYLKSRL AELNEVGTQQ ITLGNGSNDV LEILARTFVS DKDEVIFSQH
AFVVYPLVTQ AIGAKPVAVP AVDYGHDLDG MAKAVTDKTK MIFIANPNNP TGTFLSTSAL
KSFLDKIPQH IIVVLDEAYY EYVPEDQRAP SVEWIKEYPN LVVSRTFSKA YGLAGLRAGY
AVSHESVADV LNRIRQPFNM NSLSLKAAEV VLDDHAYLQK AVELNAQGMQ LLTEFCEESG
LNYIPSYGNF LTIEVGPGAE KLYDELLHEG VIVRPVGGYE LPNHLRVSIG LPEENQAFIK
AMKKLRG