(data stored in SCRATCH zone)

SWISSPROT: D4YX73_SPHJU

ID   D4YX73_SPHJU            Unreviewed;       365 AA.
AC   D4YX73;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 49.
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   ECO:0000313|EMBL:BAI94955.1};
GN   OrderedLocusNames=SJA_C1-01210 {ECO:0000313|EMBL:BAI94955.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94955.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94955.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC       (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000256|SAAS:SAAS00766437}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01023,
CC         ECO:0000256|SAAS:SAAS00766447};
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:SAAS00766412}.
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}.
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DR   EMBL; AP010803; BAI94955.1; -; Genomic_DNA.
DR   RefSeq; WP_013038775.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-01210; -.
DR   EnsemblBacteria; BAI94955; BAI94955; SJA_C1-01210.
DR   GeneID; 29271833; -.
DR   KEGG; sjp:SJA_C1-01210; -.
DR   eggNOG; ENOG4105CIH; Bacteria.
DR   eggNOG; COG0079; LUCA.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; HGFLVYR; -.
DR   OrthoDB; POG091H05S1; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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_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.
PE   3: Inferred from homology;
DR   PRODOM; D4YX73.
DR   SWISS-2DPAGE; D4YX73.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00766433};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00766461, ECO:0000313|EMBL:BAI94955.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00766428};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00766410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01023,
KW   ECO:0000256|SAAS:SAAS00766408, ECO:0000313|EMBL:BAI94955.1}.
FT   DOMAIN       28    357       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   MOD_RES     220    220       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01023}.
SQ   SEQUENCE   365 AA;  38759 MW;  63BE78AD4BDAA4E0 CRC64;
     MTKPAPKDWI LGISPYVPGK SAADDGRPLV KLSANENPLG TGDAARAALA AATADLATYP
     DPGAARLREA IAAAHGLDPA RVIYGTGSDE LLHIAASAYA GPGDEILYVR YGFSVYDIAA
     RRVGATPVVA PDADYATDVD ALLAAVTEKT KVVFLANPNN PTGTMTSREE IARLHAGLRP
     DILFVLDQAY AEYLDGQEDD GGLELAKNAS NVFVTRTFSK IYGLAAERIG WGYASVDVID
     VLHRIRAPFN VTTAGQAAAV AAVQDTAWIE ASRAHNRQWR EWLAGEVASL SNHGLRAVPS
     KANFLLILFD GKLTAEAAMK GLWDEGFATR WLPGQGLPNG LRITIGTEDQ VRKVAAKLRA
     MAEAA
//

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