ID A0A0G1GH41_9BACT Unreviewed; 367 AA.
AC A0A0G1GH41;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Histidinol-phosphate aminotransferase, histidinol-phosphate aminotransferase {ECO:0000313|EMBL:KKS98103.1};
DE EC=2.6.1.9 {ECO:0000313|EMBL:KKS98103.1};
GN ORFNames=UV73_C0003G0045 {ECO:0000313|EMBL:KKS98103.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_43_14.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618443 {ECO:0000313|EMBL:KKS98103.1, ECO:0000313|Proteomes:UP000034894};
RN [1] {ECO:0000313|EMBL:KKS98103.1, ECO:0000313|Proteomes:UP000034894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:KKS98103.1}.
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DR EMBL; LCFP01000003; KKS98103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1GH41; -.
DR STRING; 1618443.UV73_C0003G0045; -.
DR Proteomes; UP000034894; 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; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR PANTHER; PTHR43643:SF3; 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:KKS98103.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:KKS98103.1}.
FT DOMAIN 38..361
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 367 AA; 41120 MW; CB9E2AA27471C00B CRC64;
MKKQISDYLV PYIKPLTMYV SGHIDLAWKK PSLKRMMSNE NPLPPSKKVL KTVMKYASMA
NRYPDQGITV RTKIAKMNKL HGAENVVLGN GSSEIYDMIF RTFLEPGDEV IQQTPCFGIY
KLRCEVLGGK IISVPMIYRD KKLLYDAEGI INAITPKTKI IVVANPNNPT GNFMETADFI
RLAKTGIPLC IDEAYIEYEG FKKSHTKLIR KYKNVIVTRT LSKAYGLAGL RFGYLLGDRE
VAMKIAATLL PWNVGTISMW AALTALGDKK GLKDRVNYNN GERAAIIKAL SKIPGLVIFP
SKANYVLFDS GPAGKKGEDI ISFAQKKDII LRGDKPKYGS DGWFRVTVGS KAENRKFVRV
IKEFFSK
//
