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Database: UniProt
Entry: A0A1H1QQJ4_9ACTN
LinkDB: A0A1H1QQJ4_9ACTN
Original site: A0A1H1QQJ4_9ACTN 
ID   A0A1H1QQJ4_9ACTN        Unreviewed;       386 AA.
AC   A0A1H1QQJ4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000256|ARBA:ARBA00018048, ECO:0000256|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000256|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|ARBA:ARBA00030262, ECO:0000256|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000256|HAMAP-Rule:MF_01023};
GN   ORFNames=SAMN04488570_1475 {ECO:0000313|EMBL:SDS25593.1};
OS   Marmoricola scoriae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Marmoricola.
OX   NCBI_TaxID=642780 {ECO:0000313|EMBL:SDS25593.1, ECO:0000313|Proteomes:UP000198859};
RN   [1] {ECO:0000313|Proteomes:UP000198859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22127 {ECO:0000313|Proteomes:UP000198859};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC         oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC         ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01023};
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, ECO:0000256|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000256|ARBA:ARBA00007970, ECO:0000256|HAMAP-
CC       Rule:MF_01023}.
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DR   EMBL; LT629757; SDS25593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1QQJ4; -.
DR   STRING; 642780.SAMN04488570_1475; -.
DR   OrthoDB; 9809616at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000198859; Chromosome i.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01141; hisC; 1.
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.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_01023}; Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01023}; Reference proteome {ECO:0000313|Proteomes:UP000198859};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01023}.
FT   DOMAIN          36..371
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         242
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   386 AA;  41781 MW;  485628E2AEDE2DA0 CRC64;
     MSTSTQPTST ERSWVPLREE LRGVEPYGAP QLDVPVQLNV NENPYAPSAA VVEDVAASVA
     RAATTLNRYP DREFTELREG LAAYLGREAG VVVDPAQVWA ANGSNEVMLQ LLQAFGGPGR
     TAISFAPTYS MYPEYARDAM TGWVAGRRHE DFSFDLDEAR RLVREHRPSV VLLPSPNNPT
     GTALPHDVIG TLCELVGDDG VVVIDEAYAE FRRAGTPSAL ELLATADGQG HRNLVVTRTM
     SKAFALAGAR LGYLAAAPEL CDALRVVRLP YHLSAVTQAT ALAALRHADE LLGKVEELRA
     ERDRTVAWLE EQGLEVAPSD ANFVLFGRFA DRQAVWQRLL DDGVLIRVTG PEGWLRVSIG
     TAAEMQAFRS ALTGALAHPT TEGAGR
//
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