ID C7LAU8_BRUMC Unreviewed; 377 AA.
AC C7LAU8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Histidinol-phosphate aminotransferase {ECO:0000313|EMBL:ACU47633.1};
GN OrderedLocusNames=BMI_I634 {ECO:0000313|EMBL:ACU47633.1};
OS Brucella microti (strain CCM 4915).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU47633.1, ECO:0000313|Proteomes:UP000002188};
RN [1] {ECO:0000313|EMBL:ACU47633.1, ECO:0000313|Proteomes:UP000002188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU47633.1,
RC ECO:0000313|Proteomes:UP000002188};
RX PubMed=19653890; DOI=10.1186/1471-2164-10-352;
RA Audic S., Lescot M., Claverie J.-M., Scholz H.C.;
RT "Brucella microti: the genome sequence of an emerging pathogen.";
RL BMC Genomics 10:352-352(2009).
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; CP001578; ACU47633.1; -; Genomic_DNA.
DR RefSeq; WP_004689567.1; NC_013119.1.
DR AlphaFoldDB; C7LAU8; -.
DR GeneID; 58776227; -.
DR KEGG; bmr:BMI_I634; -.
DR HOGENOM; CLU_017584_3_3_5; -.
DR Proteomes; UP000002188; Chromosome 1.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:ACU47633.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:ACU47633.1}.
FT DOMAIN 38..354
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 377 AA; 40807 MW; E1FADA17B96CAFAA CRC64;
MAQPRLTPLV ESLPSTVPFI GPETLELQRG KPFKARIGAN ESSFGPAPSV IEAMRNEATE
VWKYGDPENY ALRHAIAAHH GLKAEHIMPG AGVDALLGLI VRQYVQQGDK VINSLGGYPT
FNYHVAGYGG QLVTVPYRDD KPDLDALIDA AAREKPALLY IANPDNPMGT WHEGADIQSF
IERLPETTLL ILDEAYCETA PASAFPPFET DRPNVLRMRT FSKAYGLAGI RCGYAVGNPV
AIKTFDKVRD HFAVSRMAQA AAIAALKDQA YLHEVVGKIC AGRDRIAAIA EANGLHAVAS
ATNFVAIDCG RGKDFAQAVL NGLISRDIFV RKPGTPVLDR CIRVSVGVKE QLDQFEAAFP
EALEEARKIC AANAENT
//
