MTNA_ARCFU
ID MTNA_ARCFU Reviewed; 339 AA.
AC O29877;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative 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=MTNA-like protein {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=aMTNA {ECO:0000255|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
GN OrderedLocusNames=AF_0370;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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 -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000305}.
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DR EMBL; AE000782; AAB90865.1; -; Genomic_DNA.
DR PIR; B69296; B69296.
DR RefSeq; WP_010877877.1; NC_000917.1.
DR PDB; 1T5O; X-ray; 1.90 A; A/B/C/D=2-339.
DR PDBsum; 1T5O; -.
DR AlphaFoldDB; O29877; -.
DR SMR; O29877; -.
DR STRING; 224325.AF_0370; -.
DR DNASU; 1483585; -.
DR EnsemblBacteria; AAB90865; AAB90865; AF_0370.
DR GeneID; 24793909; -.
DR KEGG; afu:AF_0370; -.
DR eggNOG; arCOG01123; Archaea.
DR HOGENOM; CLU_016218_1_2_2; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 54988at2157; -.
DR PhylomeDB; O29877; -.
DR EvolutionaryTrace; O29877; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
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..339
FT /note="Putative methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000156085"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 43..45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 241..242
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 152
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1T5O"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 109..139
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1T5O"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:1T5O"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1T5O"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:1T5O"
SQ SEQUENCE 339 AA; 37631 MW; 79BC6636690F763F CRC64;
MRSIFWDDGL KLIDQTKLPE KLEVIECRNV EELADAIKKL AVRGAPALEA AGAYGIALAA
REREFADVDE LKEHLKKAAD FLASTRPTAV NLFVGIERAL NAALKGESVE EVKELALREA
EKLAEEDVER NRKMGEYGAE LLEDGDVVLT YCNAGRLATV DWGTALGVVR SAVEQGKEIR
VIACETRPLN QGSRLTCWEL MEDGIDVTLI TDSMVGIVMQ KGMVDKVIVG ADRIVRDAVF
NKIGTYTVSV VAKHHNIPFY VAAPKATFDW ERTAKDVVIE ERPREELIFC GKRQIAPLNV
KVYNPAFDPT PLENVTALIT EYGVIYPPYE VNVPKVLKF
