HIS8_GEOMG
ID HIS8_GEOMG Reviewed; 350 AA.
AC Q39YP6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Histidinol-phosphate aminotransferase {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 {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=Gmet_0385;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) 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: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; CP000148; ABB30628.1; -; Genomic_DNA.
DR RefSeq; WP_004512357.1; NC_007517.1.
DR PDB; 3HDO; X-ray; 1.61 A; A/B=2-350.
DR PDBsum; 3HDO; -.
DR AlphaFoldDB; Q39YP6; -.
DR SMR; Q39YP6; -.
DR STRING; 269799.Gmet_0385; -.
DR EnsemblBacteria; ABB30628; ABB30628; Gmet_0385.
DR KEGG; gme:Gmet_0385; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_0_7; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR EvolutionaryTrace; Q39YP6; -.
DR Proteomes; UP000007073; 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; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..350
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000230215"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3HDO"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:3HDO"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:3HDO"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 258..281
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:3HDO"
FT TURN 323..327
FT /evidence="ECO:0007829|PDB:3HDO"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:3HDO"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:3HDO"
SQ SEQUENCE 350 AA; 39135 MW; C6158BFBB5051A99 CRC64;
MIPLRQNIAS MKGYIPGYQP PDIASWIKLN TNENPYPPSP EVVKAILEEL GPDGAALRIY
PSASSQKLRE VAGELYGFDP SWIIMANGSD EVLNNLIRAF AAEGEEIGYV HPSYSYYGTL
AEVQGARVRT FGLTGDFRIA GFPERYEGKV FFLTTPNAPL GPSFPLEYID ELARRCAGML
VLDETYAEFA ESNALELVRR HENVVVTRTL SKSYSLAGMR IGLAIARPEV IAALDKIRDH
YNLDRLAQAA CVAALRDQAY LSECCRRIRE TREWFTTELR SIGYDVIPSQ GNYLFATPPD
RDGKRVYDGL YARKVLVRHF SDPLLAHGMR ISIGTREEME QTLAALKEIG
