(data stored in SCRATCH zone)

SWISSPROT: E6V4E8_VARPE

ID   E6V4E8_VARPE            Unreviewed;       325 AA.
AC   E6V4E8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000256|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000256|HAMAP-Rule:MF_01023};
GN   OrderedLocusNames=Varpa_0472 {ECO:0000313|EMBL:ADU34694.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34694.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34694.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34694.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-
CC         yl)-2-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:0000256|HAMAP-
CC         Rule:MF_01023, ECO:0000256|SAAS:SAAS01124268};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01023,
CC         ECO:0000256|SAAS:SAAS00612749};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS00083654}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01023,
CC       ECO:0000256|SAAS:SAAS00569651}.
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DR   EMBL; CP002417; ADU34694.1; -; Genomic_DNA.
DR   RefSeq; WP_013538940.1; NC_014931.1.
DR   STRING; 595537.Varpa_0472; -.
DR   EnsemblBacteria; ADU34694; ADU34694; Varpa_0472.
DR   GeneID; 29719978; -.
DR   KEGG; vpe:Varpa_0472; -.
DR   eggNOG; ENOG4105CIH; Bacteria.
DR   eggNOG; COG0079; LUCA.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; HGFLVYR; -.
DR   OrthoDB; 1248286at2; -.
DR   BioCyc; VPAR595537:G1GQO-473-MONOMER; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000008917; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; E6V4E8.
DR   SWISS-2DPAGE; E6V4E8.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00458739};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00458699, ECO:0000313|EMBL:ADU34694.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00458814};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00473492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00458799, ECO:0000313|EMBL:ADU34694.1}.
FT   DOMAIN        1    323       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   MOD_RES     192    192       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01023}.
SQ   SEQUENCE   325 AA;  34533 MW;  1E8074AA2304FB20 CRC64;
     MILLASNENP LGMPESARRA AAAALEGAGN YPDSNGTALK NALAARLDVS PEWLTLGSGS
     SEILELAAQV SLKPGENVVY SQYGFIVYAQ ATAHAHARAS VVPSQDFGHD LGAMRAAIAD
     DTKLVFVANP NNPTGTFIDA GPLRDFLQSV PAHVTVLLDE AYTEYLSPAQ RYDSIEWVRR
     LPNLIVARTF SKAFGLAGMR IGYGVSQPPL TSRMNAQRPR FNVTTPAQAA AVAALGDTEF
     LARTYELNTA GREQLAAGFT ELGLVHIPSS GNFLMVQVGD AQAVHARLLA AGIEVSLLGP
     YGLPQWLRVS VGLPEQNEAL LAALR
//

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