ID A0A086Y456_9RHOB Unreviewed; 371 AA.
AC A0A086Y456;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Histidinol-phosphate aminotransferase {ECO:0000313|EMBL:KFI29056.1};
DE EC=2.6.1.9 {ECO:0000313|EMBL:KFI29056.1};
GN ORFNames=CG50_12775 {ECO:0000313|EMBL:KFI29056.1};
OS Paenirhodobacter enshiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paenirhodobacter.
OX NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI29056.1, ECO:0000313|Proteomes:UP000028824};
RN [1] {ECO:0000313|EMBL:KFI29056.1, ECO:0000313|Proteomes:UP000028824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW2-9 {ECO:0000313|EMBL:KFI29056.1,
RC ECO:0000313|Proteomes:UP000028824};
RA Wang D., Wang G.;
RT "Genome of Paenirhodobacter enshiensis DW2-9.";
RL Submitted (MAR-2014) 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 -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000256|ARBA:ARBA00007970}.
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:KFI29056.1}.
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DR EMBL; JFZB01000005; KFI29056.1; -; Genomic_DNA.
DR RefSeq; WP_036635632.1; NZ_JFZB01000005.1.
DR AlphaFoldDB; A0A086Y456; -.
DR STRING; 1105367.CG50_12775; -.
DR eggNOG; COG0079; Bacteria.
DR OrthoDB; 9809616at2; -.
DR Proteomes; UP000028824; 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; 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; 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 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KFI29056.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000028824};
KW Transferase {ECO:0000313|EMBL:KFI29056.1}.
FT DOMAIN 37..359
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 371 AA; 39449 MW; D160310A03F2313D CRC64;
MTGPRYTPLI DSLPSTVPFV GPETQERRMG HPFAARLGAN ENGFGPSPRA IAAMAAAAGE
VWKYGDPENH DLRKALAEKH DCDPANIVVG EGIDGLLGYL VRLVIAPGDR VVTSEGAYPT
FNFHVAGYGG ELHKVPYKGD HEDPDALIAL AKQVGPKLIY IANPDNPMAS AHPGETILRM
VEQVPEGALL VLDEAYVDLA PEGTAPAIPA DDPRVIRFRT FSKAHGMAGA RVGYAIGAKP
LIAAFDKIRN HFGMSRISQA GALASLQDKT WQAYMRRLIA ASRDRIGEIA AENGLSALPS
ATNFVAIDCG RDGTFARAVL EELTGAGIFV RMPGVAPQDR CIRVSCGPEP EMEAFAAALP
GALDRARARL G
//
