HIS82_TRIV2
ID HIS82_TRIV2 Reviewed; 380 AA.
AC Q3MAX6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Histidinol-phosphate aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01023};
DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE AltName: Full=Imidazole acetol-phosphate transaminase 2 {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC2 {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=Ava_2242;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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:0000255|HAMAP-
CC Rule:MF_01023};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01023}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR EMBL; CP000117; ABA21860.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3MAX6; -.
DR SMR; Q3MAX6; -.
DR STRING; 240292.Ava_2242; -.
DR EnsemblBacteria; ABA21860; ABA21860; Ava_2242.
DR KEGG; ava:Ava_2242; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_3; -.
DR OMA; YPDMACT; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000002533; Chromosome.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1.
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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..380
FT /note="Histidinol-phosphate aminotransferase 2"
FT /id="PRO_0000230202"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 380 AA; 41730 MW; 97124B9B0046E6C7 CRC64;
MLPFIRSDLA QFTAYKPHPS SDTDAAVPAQ LDRLDTNESP CDLPPELKQK LAWTFQQVIE
SNRYPDGGHE ELKDAIAQYV NESANISSSP ITAANISVGN GSDELIRSLL IATCLGAQGS
ILVANPTFSM YGILAQTLGI PVVTVSRNPE NFEIDLTAAQ SAIEQTQNPP IRVVFVVHPN
SPTANPLTTN ELRWLKSLSE QILVVVDEAY FEFSQTTLIS ELVQRPNWVI LRTFSKAFRL
AAMRVGYCVA HPEAIAILEK VRLPYNLPSF SITSALVALQ NRAILLESIP QILNERAKLI
TALSKYPELA VAESAANFIF LQLKTDNKNS PDTALLNLHQ QLKNSGTLVR QISGGLRITI
GTPEENIRTL NHIQTALIKA
