HIS82_NOSS1
ID HIS82_NOSS1 Reviewed; 384 AA.
AC Q8YMG7;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Histidinol-phosphate aminotransferase 2;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase 2;
GN Name=hisC2; OrderedLocusNames=all4966;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000019; BAB76665.1; -; Genomic_DNA.
DR PIR; AF2426; AF2426.
DR RefSeq; WP_010999092.1; NZ_RSCN01000018.1.
DR AlphaFoldDB; Q8YMG7; -.
DR SMR; Q8YMG7; -.
DR STRING; 103690.17134104; -.
DR EnsemblBacteria; BAB76665; BAB76665; BAB76665.
DR KEGG; ana:all4966; -.
DR eggNOG; COG0079; Bacteria.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000002483; 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..384
FT /note="Histidinol-phosphate aminotransferase 2"
FT /id="PRO_0000153294"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 42118 MW; 436A87712C768DEA CRC64;
MLPFIRSDLA QFNAYKPHPS SDTASAVPPQ LDRLDTNESP YDLPPELKQK LAWTFQQVIE
SNRYPDGGHE TLKSAIAEYV NESANISSLR FTAANISVGN GSDELIRSLL IATCLSGEGS
ILVANPTFSM YGILAQTLGI PVVSVSRNPD NFAIDLTAAQ SAIEQTLNPP IRVVFVVHPN
SPTANPLTAN ELRWLKSLSE RILVVVDEAY FEFSQNTLVS ELAQRPNWII LRTFSKAFRL
AAMRVGYCVA HPEAIAILEK VRLPYNLPSF SIASALVALQ NRAILLESIP QTLDERTKLI
NAFSQHPALA VAESAANFIF LRLKADSDNS SDTTLLNLHQ QLKNSGTLVR QISGGLRITI
GTPEENIRTL NHIQTALIKP ELVG