ID C7DB17_9RHOB Unreviewed; 369 AA.
AC C7DB17;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Histidinol-phosphate aminotransferase {ECO:0000313|EMBL:EET49466.1};
DE EC=2.6.1.9 {ECO:0000313|EMBL:EET49466.1};
GN ORFNames=TR2A62_1755 {ECO:0000313|EMBL:EET49466.1};
OS Thalassobium sp. R2A62.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassobium.
OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET49466.1, ECO:0000313|Proteomes:UP000004701};
RN [1] {ECO:0000313|EMBL:EET49466.1, ECO:0000313|Proteomes:UP000004701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2A62 {ECO:0000313|EMBL:EET49466.1,
RC ECO:0000313|Proteomes:UP000004701};
RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
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 -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR EMBL; GG697169; EET49466.1; -; Genomic_DNA.
DR RefSeq; WP_009160519.1; NZ_GG697169.2.
DR AlphaFoldDB; C7DB17; -.
DR STRING; 633131.TR2A62_1755; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_5; -.
DR OrthoDB; 9809616at2; -.
DR Proteomes; UP000004701; Unassembled WGS sequence.
DR GO; GO:0004400; F:histidinol-phosphate transaminase 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EET49466.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000004701};
KW Transferase {ECO:0000313|EMBL:EET49466.1}.
FT DOMAIN 37..359
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 369 AA; 39080 MW; A3E07EA426681242 CRC64;
MTQPQLTPLA QKLPSTVPFV GPETQERARG SVFSARLGAN ESSFGPSPLV IAAMQAAASD
TWMYGDPENY DLRSALSRAY GTPMENIVVG EGIDGLLGYL VRLFISDGDA VVTSAGAYPT
FNYHVAGFGG VVHAVPYRDD HEDPAALIAK AIEVGAKLIY FANPDNPMGT HHSAETVLEM
IAKVPSDCLL ILDEAYVELA PEGTAPTFDP NTPNVIRMRT FSKAYGMAGA RVGHAIGPVD
LITAFGKIRN HFGMSRIGQA GALAAIADTA YLEDIRGKVA AARGRISQIA ADNGLSIIPS
ATNFVAVDCG QDGDFARRVL AELIARDLFV RMPFVAPQDR CIRVSCGTPS QMDQLAAALP
EALIAARSS
//
