MTNA_THEMA
ID MTNA_THEMA Reviewed; 343 AA.
AC Q9X013;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
GN Name=mtnA {ECO:0000255|HAMAP-Rule:MF_01678}; OrderedLocusNames=TM_0911;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SULFATE IONS.
RG Midwest center for structural genomics (MCSG);
RT "X-ray crystal structure of aif-2b translation initiation factor from
RT Thermotoga maritima.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_01678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01678};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 1/6. {ECO:0000255|HAMAP-Rule:MF_01678}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35992.1; -; Genomic_DNA.
DR PIR; F72319; F72319.
DR RefSeq; NP_228719.1; NC_000853.1.
DR RefSeq; WP_004080652.1; NZ_CP011107.1.
DR PDB; 1T9K; X-ray; 2.60 A; A/B/C/D=1-343.
DR PDBsum; 1T9K; -.
DR AlphaFoldDB; Q9X013; -.
DR SMR; Q9X013; -.
DR STRING; 243274.THEMA_00080; -.
DR EnsemblBacteria; AAD35992; AAD35992; TM_0911.
DR KEGG; tma:TM0911; -.
DR eggNOG; COG0182; Bacteria.
DR InParanoid; Q9X013; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1290468at2; -.
DR UniPathway; UPA00904; UER00874.
DR EvolutionaryTrace; Q9X013; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR005251; IF-M1Pi.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Isomerase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..343
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000156094"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 48..50
FT /ligand="substrate"
FT BINDING 88
FT /ligand="substrate"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 244..245
FT /ligand="substrate"
FT SITE 154
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1T9K"
FT TURN 20..25
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:1T9K"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 114..141
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1T9K"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1T9K"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:1T9K"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1T9K"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:1T9K"
SQ SEQUENCE 343 AA; 38050 MW; 462EB159438C5BEF CRC64;
MKLKTKTMEW SGNSLKLLDQ RKLPFIEEYV ECKTHEEVAH AIKEMIVRGA PAIGVAAAFG
YVLGLRDYKT GSLTDWMKQV KETLARTRPT AVNLFWALNR MEKVFFENAD RENLFEILEN
EALKMAYEDI EVNKAIGKNG AQLIKDGSTI LTHCNAGALA TVDYGTALGV IRAAVESGKR
IRVFADETRP YLQGARLTAW ELMKDGIEVY VITDNMAGWL MKRGLIDAVV VGADRIALNG
DTANKIGTYS LAVLAKRNNI PFYVAAPVST IDPTIRSGEE IPIEERRPEE VTHCGGNRIA
PEGVKVLNPA FDVTENTLIT AIITEKGVIR PPFEENIKKI LEV
