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Database: UniProt
Entry: A0A218Q4Q2_9CYAN
LinkDB: A0A218Q4Q2_9CYAN
Original site: A0A218Q4Q2_9CYAN 
ID   A0A218Q4Q2_9CYAN        Unreviewed;       350 AA.
AC   A0A218Q4Q2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Histidinol-phosphate aminotransferase {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|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000256|HAMAP-Rule:MF_01023};
GN   ORFNames=NIES3585_28930 {ECO:0000313|EMBL:GAX36854.1};
OS   Nodularia sp. NIES-3585.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Nodularia.
OX   NCBI_TaxID=1973477 {ECO:0000313|EMBL:GAX36854.1, ECO:0000313|Proteomes:UP000198352};
RN   [1] {ECO:0000313|EMBL:GAX36854.1, ECO:0000313|Proteomes:UP000198352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3585 {ECO:0000313|EMBL:GAX36854.1,
RC   ECO:0000313|Proteomes:UP000198352};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01023}.
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:GAX36854.1}.
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DR   EMBL; BDUB01000001; GAX36854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218Q4Q2; -.
DR   OrthoDB; 9813612at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000198352; Unassembled WGS sequence.
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; PTHR43643:SF3; 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   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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01023}.
FT   DOMAIN          27..345
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   350 AA;  38775 MW;  AEB08E1FB39E89D4 CRC64;
     MTNYFRSNID AMASYVPGEQ PQRGIQTIKL NSNENPYPPS PAVLAVLKNI EGEWLRRYPE
     PLGGEFRRAA SKVLGVPSDW IIVGNGSDEV LNLVIRACTE PGKKVVYPIP TYVLYVTLTQ
     MQGAELVEIP YGEDYKLPLE EIIAANGSVT FIASPNSPSG HIVPIDDLRQ LASRLAGVLV
     IDEAYVDFAE ENALALVKEY ENVIVIRTLS KGYSLAGLRL GFGVANPRLL HGLFKVKDSY
     NIDAIACTLG TAAITDQDYK NACVAKVKAS RTQLATDLKK LNFQVWDSQT NFLLVQPPQE
     NAEYLYQQLK ERQILVRYFP QPGLDNKLRI TVGTDAQNQI LIETLSQICS
//
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