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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Histidinol-phosphate aminotransferase 1; EC=2.6.1.9; AltName: Full=Imidazole acetol-phosphate transaminase 1; |
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| MyHits synonyms | HIS81_BACCR , Q81FQ1 , 5CF1BD42152BC048 |
 Legends: 1, N6-(pyridoxal phosphate)lysine. {ECO:0000250}; 2, ipat:AA_TRANSFER_CLASS_2 [T].
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ID HIS81_BACCR Reviewed; 370 AA.
AC Q81FQ1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 12-APR-2017, entry version 91.
DE RecName: Full=Histidinol-phosphate aminotransferase 1;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN Name=hisC1; OrderedLocusNames=BC_1518;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 /
OS NCIMB 9373 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with
RT Bacillus anthracis.";
RL Nature 423:87-91(2003).
CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine 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; AE016877; AAP08498.1; -; Genomic_DNA.
DR RefSeq; NP_831297.1; NC_004722.1.
DR RefSeq; WP_001264019.1; NC_004722.1.
DR ProteinModelPortal; Q81FQ1; -.
DR SMR; Q81FQ1; -.
DR STRING; 226900.BC1518; -.
DR PRIDE; Q81FQ1; -.
DR EnsemblBacteria; AAP08498; AAP08498; BC_1518.
DR GeneID; 1203867; -.
DR KEGG; bce:BC1518; -.
DR PATRIC; 32598772; VBIBacCer54481_1495.
DR eggNOG; COG0079; LUCA.
DR KO; K00817; -.
DR OMA; YPSEANY; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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; Complete proteome;
KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1 370 Histidinol-phosphate aminotransferase 1.
FT /FTId=PRO_0000153301.
FT MOD_RES 222 222 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 30 352 ipfam:Aminotran_1_2 [T]
FT MYHIT 219 228 ipat:AA_TRANSFER_CLASS_2 [T]
FT MYHIT 2 359 ihamap:HisC_aminotrans_2 [T]
SQ SEQUENCE 370 AA; 41620 MW; 5CF1BD42152BC048 CRC64;
MRVKEQLLTL RAYVPGKNIE EVKREYGLSK IVKLASNENP FGCSARVTEA LTSLASQYAL
YPDGYAFELR TKIAEHLGVK AEQLLFGSGL DEVIQMISRA LLHEGTNVVM ANPTFSQYHH
HAVIEGAEVR EVSLKDGIHD LDAMLEQVDE KTKIVWICNP NNPTGTYVEK QKLLSFLESV
PKSALVIMDE AYYEYAEAED YPQTLPLLEK YENLMVLRTF SKAYGLAAFR IGYAIGDAKL
IGQLEVARLP FNTSTVAQSV ALAALEDQAF LQDCVQKNAE GLNQYYAFCK EYNVFYYPSQ
TNFIFLKLGI PGNEAFERLM KKGYIVRSGA AFGIDDGIRI TVGLKEENDE IIELLKELVN
EQVQKEETYS
//
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