PUR9_MYCTU
ID PUR9_MYCTU Reviewed; 523 AA.
AC P9WHM7; L0T5A3; P67541; P71553;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139};
DE EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139};
DE EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139};
GN Name=purH {ECO:0000255|HAMAP-Rule:MF_00139}; OrderedLocusNames=Rv0957;
GN ORFNames=MTCY10D7.17c;
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 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=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP-
CC Rule:MF_00139, 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; CCP43705.1; -; Genomic_DNA.
DR PIR; C70717; C70717.
DR RefSeq; NP_215472.1; NC_000962.3.
DR RefSeq; WP_003404890.1; NZ_NVQJ01000001.1.
DR PDB; 3ZZM; X-ray; 2.20 A; A/B=1-523.
DR PDB; 4A1O; X-ray; 2.48 A; A/B=1-523.
DR PDBsum; 3ZZM; -.
DR PDBsum; 4A1O; -.
DR AlphaFoldDB; P9WHM7; -.
DR SMR; P9WHM7; -.
DR STRING; 83332.Rv0957; -.
DR PaxDb; P9WHM7; -.
DR DNASU; 885406; -.
DR GeneID; 885406; -.
DR KEGG; mtu:Rv0957; -.
DR TubercuList; Rv0957; -.
DR eggNOG; COG0138; Bacteria.
DR OMA; WRVAKFV; -.
DR PhylomeDB; P9WHM7; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_00139; PurH; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692; PTHR11692; 1.
DR Pfam; PF01808; AICARFT_IMPCHas; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Multifunctional enzyme; Purine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..523
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_0000192106"
FT DOMAIN 1..152
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:3ZZM"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:3ZZM"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:3ZZM"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 171..198
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4A1O"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 274..283
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 286..295
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 408..420
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 476..484
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:3ZZM"
FT HELIX 499..509
FT /evidence="ECO:0007829|PDB:3ZZM"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:3ZZM"
SQ SEQUENCE 523 AA; 55026 MW; 5A78C034101019C7 CRC64;
MSTDDGRRPI RRALISVYDK TGLVDLAQGL SAAGVEIIST GSTAKTIADT GIPVTPVEQL
TGFPEVLDGR VKTLHPRVHA GLLADLRKSE HAAALEQLGI EAFELVVVNL YPFSQTVESG
ASVDDCVEQI DIGGPAMVRA AAKNHPSAAV VTDPLGYHGV LAALRAGGFT LAERKRLASL
AFQHIAEYDI AVASWMQQTL APEHPVAAFP QWFGRSWRRV AMLRYGENPH QQAALYGDPT
AWPGLAQAEQ LHGKDMSYNN FTDADAAWRA AFDHEQTCVA IIKHANPCGI AISSVSVADA
HRKAHECDPL SAYGGVIAAN TEVSVEMAEY VSTIFTEVIV APGYAPGALD VLARKKNIRV
LVAAEPLAGG SELRPISGGL LIQQSDQLDA HGDNPANWTL ATGSPADPAT LTDLVFAWRA
CRAVKSNAIV IAADGATVGV GMGQVNRVDA ARLAVERGGE RVRGAVAASD AFFPFPDGLE
TLAAAGVTAV VHPGGSVRDE EVTEAAAKAG VTLYLTGARH FAH
