ID A0A256Z9X5_9ARCH Unreviewed; 349 AA.
AC A0A256Z9X5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Putative methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_01678};
DE AltName: Full=MTNA-like protein {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=aMTNA {ECO:0000256|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
GN Name=mtnA {ECO:0000313|EMBL:OYT49468.1};
GN ORFNames=B6U79_01705 {ECO:0000313|EMBL:OYT49468.1};
OS Candidatus Bathyarchaeota archaeon ex4484_231.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2012512 {ECO:0000313|EMBL:OYT49468.1, ECO:0000313|Proteomes:UP000216686};
RN [1] {ECO:0000313|Proteomes:UP000216686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01678};
CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYT49468.1}.
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DR EMBL; NJDZ01000024; OYT49468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256Z9X5; -.
DR Proteomes; UP000216686; Unassembled WGS sequence.
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; translation initiation factor eif-2b, domain 1; 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 NCBIfam; TIGR00524; eIF-2B_rel; 1.
DR NCBIfam; TIGR00512; salvage_mtnA; 1.
DR PANTHER; PTHR43475; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR43475:SF1; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01678};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678}.
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 50..52
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 249..250
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 160
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 349 AA; 38843 MW; 019218DFEB451A80 CRC64;
MTVVKLMRTI TWDNGVVVTI DQTVLPNKEI WLELKTCREV AEALKEMKMR GAPLIGVAAA
YGMALTAYHS RAKERKDLFR ELEQSAEVLR NTRPTAVNLF WAVERVLNKA KKTEGDVETL
KKAVVEEAQR MADEDVEINR MIGKNGAKLI EDGDVVLTHC NAGSLATVDY GTALAVIRAA
WEEGKRIRVV ADETRPKLQG ARLTAYELMR DGIPVTLITD NMAGYLMSKG LINKVVVGAD
RIVQDGVANK IGTYTVAVLA HEHKIPFYVA APVSTFDLTR RSQEVIIEER DPKEVTHIQS
IRIAPEGVAV MNPAFDITPL KYVDAIICEK GVLSREEFRK LAREKCSKN
//
