MTNA_PYRHO
ID MTNA_PYRHO Reviewed; 364 AA.
AC O58433;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-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=PH0702;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29793.1; -; Genomic_DNA.
DR PIR; G71116; G71116.
DR RefSeq; WP_010884797.1; NC_000961.1.
DR PDB; 6A34; X-ray; 2.30 A; A/B=1-364.
DR PDB; 6A35; X-ray; 2.65 A; A/B/C/D=1-364.
DR PDBsum; 6A34; -.
DR PDBsum; 6A35; -.
DR AlphaFoldDB; O58433; -.
DR SMR; O58433; -.
DR STRING; 70601.3257110; -.
DR EnsemblBacteria; BAA29793; BAA29793; BAA29793.
DR GeneID; 1443032; -.
DR KEGG; pho:PH0702; -.
DR eggNOG; arCOG01123; Archaea.
DR OMA; RLWVDET; -.
DR OrthoDB; 54988at2157; -.
DR BRENDA; 5.3.1.23; 5244.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..364
FT /note="Putative methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000156090"
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 57..59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 257..258
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 167
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:6A34"
FT TURN 29..34
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:6A34"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 125..157
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:6A34"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:6A34"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6A34"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:6A34"
SQ SEQUENCE 364 AA; 40380 MW; EE3B6A00A2D61F9D CRC64;
MEIRYTPKEL TKLPRTVEYK NKSVYMINQR LLPKEFKVEK FSKVEEVAEA IKNMTVRGAP
AIGAAAGFGL ALYAETSKAK TKEEFLDGFE KAYEILKNTR PTAVNLFWAL NRIKKLVEEH
SEDPLDEIKR LIVQEAYKIA DEDVEANLRM GHYGAEVLPE GNILTHCNAG SLATVHLGTV
GSVVRVMHKD GSLKLLWLDE TRPVLQGARL SAWEYSYDGL NVKLIADNAA AFVMQQGFVD
AIIVGADRIV ANGDFANKIG TYMLAVLARE HGIPFFAVAP LSSIDMELKS GKDIPIEERS
PEEVLTCGGC RIAPDVPVYN PAFDVTPHKY LTGIITDRGV VWPPFKRNLK KLFEVNKSGG
DEAV
