ID G0EH79_PYRF1 Unreviewed; 355 AA.
AC G0EH79;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Histidinol-phosphate aminotransferase {ECO:0000313|EMBL:AEM39303.1};
GN OrderedLocusNames=Pyrfu_1445 {ECO:0000313|EMBL:AEM39303.1};
OS Pyrolobus fumarii (strain DSM 11204 / 1A).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrolobus.
OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM39303.1, ECO:0000313|Proteomes:UP000001037};
RN [1] {ECO:0000313|EMBL:AEM39303.1, ECO:0000313|Proteomes:UP000001037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX PubMed=21886865;
RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT Pyrolobus fumarii type strain (1A).";
RL Stand. Genomic Sci. 4:381-392(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC {ECO:0000256|ARBA:ARBA00005011}.
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DR EMBL; CP002838; AEM39303.1; -; Genomic_DNA.
DR RefSeq; WP_014026980.1; NC_015931.1.
DR AlphaFoldDB; G0EH79; -.
DR STRING; 694429.Pyrfu_1445; -.
DR GeneID; 11138631; -.
DR KEGG; pfm:Pyrfu_1445; -.
DR eggNOG; arCOG04273; Archaea.
DR HOGENOM; CLU_017584_3_1_2; -.
DR InParanoid; G0EH79; -.
DR OrthoDB; 39225at2157; -.
DR Proteomes; UP000001037; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR01141; hisC; 1.
DR PANTHER; PTHR42885:SF2; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:AEM39303.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001037};
KW Transferase {ECO:0000313|EMBL:AEM39303.1}.
FT DOMAIN 28..346
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 355 AA; 39833 MW; 47E9390F077C8F65 CRC64;
MSVREFAKDG FLDATPYPLP KRHPGITYLD LNECPFEPPA FVQEAVCKAA RRGNRYPTLD
DYYTVERLIA DYAGLEPDYV VLTAGGDEAL RAIFDVFVGP GDRVVLLEPG FAMTRFYTIV
RGGVYQAVKL REEGRRFLLD ENELLEVASG ARMIVIENPH NPTGSLLANE ELAIRLLDET
DAIVVFDEAY YEFAGLSIAR LTQRYDRLIV VRTLSKAFCL AGYRVGYILA HPTASELLRK
ALTPFNLSVV QLAAAQAALE NRDYVEKVIA HVNSEKDRMT KRLEELGLRV YESYTNFLLV
KTGVPDIHEL LAKHGVVVKQ IKSLGSDYIR VTIGTREEND KFIHAIEQAV ASVTR
//
