HIS8_MYCTU
ID HIS8_MYCTU Reviewed; 380 AA.
AC P9WML7; L0T9Y3; O06591; P0A678;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Histidinol-phosphate aminotransferase;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase;
GN Name=hisC; Synonyms=hisC1; OrderedLocusNames=Rv1600; ORFNames=MTCY336.04c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44364.1; -; Genomic_DNA.
DR PIR; B70544; B70544.
DR RefSeq; WP_003407947.1; NZ_NVQJ01000016.1.
DR RefSeq; YP_177823.1; NC_000962.3.
DR PDB; 4R8D; X-ray; 2.05 A; A/B=1-380.
DR PDB; 4RAE; X-ray; 2.59 A; A/B=1-380.
DR PDBsum; 4R8D; -.
DR PDBsum; 4RAE; -.
DR AlphaFoldDB; P9WML7; -.
DR SMR; P9WML7; -.
DR STRING; 83332.Rv1600; -.
DR PaxDb; P9WML7; -.
DR DNASU; 886298; -.
DR GeneID; 886298; -.
DR KEGG; mtu:Rv1600; -.
DR TubercuList; Rv1600; -.
DR eggNOG; COG0079; Bacteria.
DR OMA; IWLNANE; -.
DR PhylomeDB; P9WML7; -.
DR BRENDA; 2.6.1.9; 3445.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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..380
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153397"
FT MOD_RES 232
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4RAE"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:4R8D"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4R8D"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4RAE"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:4R8D"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:4R8D"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4R8D"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 278..301
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:4R8D"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:4R8D"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:4R8D"
SQ SEQUENCE 380 AA; 40581 MW; 490B2865E361587A CRC64;
MTRSGHPVTL DDLPLRADLR GKAPYGAPQL AVPVRLNTNE NPHPPTRALV DDVVRSVREA
AIDLHRYPDR DAVALRADLA GYLTAQTGIQ LGVENIWAAN GSNEILQQLL QAFGGPGRSA
IGFVPSYSMH PIISDGTHTE WIEASRANDF GLDVDVAVAA VVDRKPDVVF IASPNNPSGQ
SVSLPDLCKL LDVAPGIAIV DEAYGEFSSQ PSAVSLVEEY PSKLVVTRTM SKAFAFAGGR
LGYLIATPAV IDAMLLVRLP YHLSSVTQAA ARAALRHSDD TLSSVAALIA ERERVTTSLN
DMGFRVIPSD ANFVLFGEFA DAPAAWRRYL EAGILIRDVG IPGYLRATTG LAEENDAFLR
ASARIATDLV PVTRSPVGAP
