HIS82_BRADU
ID HIS82_BRADU Reviewed; 365 AA.
AC Q89UL9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=bll1397;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC46662.1; -; Genomic_DNA.
DR RefSeq; NP_768037.1; NC_004463.1.
DR RefSeq; WP_011084214.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89UL9; -.
DR SMR; Q89UL9; -.
DR STRING; 224911.27349649; -.
DR EnsemblBacteria; BAC46662; BAC46662; BAC46662.
DR GeneID; 64021267; -.
DR KEGG; bja:bll1397; -.
DR PATRIC; fig|224911.44.peg.820; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_5; -.
DR InParanoid; Q89UL9; -.
DR OMA; YPDMACT; -.
DR PhylomeDB; Q89UL9; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000002526; 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..365
FT /note="Histidinol-phosphate aminotransferase 2"
FT /id="PRO_0000153326"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 39892 MW; 890FB3D6A7678269 CRC64;
MSCPVPNPGI LDIAPYTPGK SPVPEPGRKV FKLSANETPF GPSPKAIEAF KKVADHLEDY
PEGTSRVLRE AIGRTFGLDP NRIICGAGSD EILNLLAHTY LGQGDEAIST THGFLVYPIA
TMAVGARNVI AQEKNLTCDV DAILKAVTPK TKLVWLANPN NPTGTYIPFD EVKRLRAGLP
SHVLLVLDAA YCDYVSRNDY EMGIELVATT ENTVVTHTFS KIHGLAALRI GWMFGPEHII
DAVNRIRGPF NVSTPAMYAA VAAIEDTAHQ AMSKQFTETW RNWLTEEIGK LGLKVTPSVA
NFVLIHFPTD RGRTSDDADA FLTKRGLVLR ALKNYGLPHS LRMTIGTEEA NRLVVDGLRD
FMAGK