ID A0A017HQ82_9RHOB Unreviewed; 308 AA.
AC A0A017HQ82;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Histidinol-phosphate aminotransferase / Aromatic-amino-acid aminotransferase {ECO:0000313|EMBL:EYD76516.1};
DE EC=2.6.1.57 {ECO:0000313|EMBL:EYD76516.1};
DE EC=2.6.1.9 {ECO:0000313|EMBL:EYD76516.1};
GN ORFNames=Rumeso_01937 {ECO:0000313|EMBL:EYD76516.1};
OS Rubellimicrobium mesophilum DSM 19309.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD76516.1, ECO:0000313|Proteomes:UP000019666};
RN [1] {ECO:0000313|EMBL:EYD76516.1, ECO:0000313|Proteomes:UP000019666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD76516.1,
RC ECO:0000313|Proteomes:UP000019666};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYD76516.1}.
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DR EMBL; AOSK01000043; EYD76516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A017HQ82; -.
DR STRING; 442562.Rumeso_01937; -.
DR PATRIC; fig|442562.3.peg.1913; -.
DR HOGENOM; CLU_017584_3_3_5; -.
DR Proteomes; UP000019666; Unassembled WGS sequence.
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:0009058; P: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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43643:SF6; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EYD76516.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019666};
KW Transferase {ECO:0000313|EMBL:EYD76516.1}.
FT DOMAIN 2..289
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 308 AA; 32575 MW; 8E791ADDFE32DB1C CRC64;
MYGDPEVHEL REAIAALHGV DPGQVIVGEG IDGLLGLLVR LTVGAGVPVV TSLGAYPTFN
FHVTGFGGRL LTMPYKGDAS DPEALLSLAR ESRARLIYLS NPDNPMGSMH GPEAIRRMVE
GAPEGALLVL DEAYAELAPE GSLPEIDPED ARVIRFRTFS KAHGLAGLRV GYGIGPRALV
AAFDRVRNHF GLGRVAQAGA LAAVLDREWP AEVARLVAEG REEIGRIARA AALRPLPSSA
NFVAVDCGRD GAFARAVLEG LGRRGVFVRM PGVAPLDRCI RVTVGRPEAL AVFGAALPEA
LEEARGRT
//
