HIS4_MYCTU
ID HIS4_MYCTU Reviewed; 244 AA.
AC P9WMM5; L0T7E1; O06588; P60578;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Phosphoribosyl isomerase A;
DE AltName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE EC=5.3.1.16;
DE AltName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE Short=PRAI;
DE EC=5.3.1.24;
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN Name=priA; Synonyms=hisA; OrderedLocusNames=Rv1603;
GN ORFNames=MTCY336.01c, MTV046.01;
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 INVOLVEMENT IN HISTIDINE AND TRYPTOPHAN BIOSYNTHESIS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12634849; DOI=10.1038/sj.embor.embor771;
RA Barona-Gomez F., Hodgson D.A.;
RT "Occurrence of a putative ancient-like isomerase involved in histidine and
RT tryptophan biosynthesis.";
RL EMBO Rep. 4:296-300(2003).
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 -!- FUNCTION: Involved in both the histidine and tryptophan biosynthetic
CC pathways.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP44367.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44367.1; ALT_INIT; Genomic_DNA.
DR PIR; E70544; E70544.
DR RefSeq; NP_216119.1; NC_000962.3.
DR PDB; 2Y85; X-ray; 2.40 A; A/B/C/D=1-244.
DR PDB; 2Y88; X-ray; 1.33 A; A=1-244.
DR PDB; 2Y89; X-ray; 2.50 A; A=1-244.
DR PDB; 3ZS4; X-ray; 1.90 A; A=1-244.
DR PDBsum; 2Y85; -.
DR PDBsum; 2Y88; -.
DR PDBsum; 2Y89; -.
DR PDBsum; 3ZS4; -.
DR AlphaFoldDB; P9WMM5; -.
DR SMR; P9WMM5; -.
DR STRING; 83332.Rv1603; -.
DR PaxDb; P9WMM5; -.
DR DNASU; 885873; -.
DR GeneID; 885873; -.
DR KEGG; mtu:Rv1603; -.
DR PATRIC; fig|83332.12.peg.1785; -.
DR TubercuList; Rv1603; -.
DR eggNOG; COG0106; Bacteria.
DR OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:MTBBASE.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:MTBBASE.
DR CDD; cd04732; HisA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01014; HisA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR010188; HisA/PriA_Actinobacteria.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR023016; Isoase_HisA-like_bact.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01919; hisA-trpF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cytoplasm; Histidine biosynthesis; Isomerase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..244
FT /note="Phosphoribosyl isomerase A"
FT /id="PRO_0000142085"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2Y88"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2Y88"
FT TURN 171..177
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:2Y88"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:2Y88"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2Y88"
SQ SEQUENCE 244 AA; 25632 MW; 8B9C2C403958A01E CRC64;
MPLILLPAVD VVEGRAVRLV QGKAGSQTEY GSAVDAALGW QRDGAEWIHL VDLDAAFGRG
SNHELLAEVV GKLDVQVELS GGIRDDESLA AALATGCARV NVGTAALENP QWCARVIGEH
GDQVAVGLDV QIIDGEHRLR GRGWETDGGD LWDVLERLDS EGCSRFVVTD ITKDGTLGGP
NLDLLAGVAD RTDAPVIASG GVSSLDDLRA IATLTHRGVE GAIVGKALYA RRFTLPQALA
AVRD
