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Database: UniProt
Entry: A0A0Q4R389_9BACL
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ID   A0A0Q4R389_9BACL        Unreviewed;       351 AA.
AC   A0A0Q4R389;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=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=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
GN   Name=mtnA {ECO:0000256|HAMAP-Rule:MF_01678,
GN   ECO:0000313|EMBL:KQO01252.1};
GN   ORFNames=ASF12_15550 {ECO:0000313|EMBL:KQO01252.1};
OS   Paenibacillus sp. Leaf72.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO01252.1, ECO:0000313|Proteomes:UP000051722};
RN   [1] {ECO:0000313|EMBL:KQO01252.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO01252.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO01252.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO01252.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- 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:0000256|HAMAP-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:KQO01252.1}.
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DR   EMBL; LMLV01000030; KQO01252.1; -; Genomic_DNA.
DR   RefSeq; WP_056039749.1; NZ_LMLV01000030.1.
DR   AlphaFoldDB; A0A0Q4R389; -.
DR   STRING; 1736234.ASF12_15550; -.
DR   OrthoDB; 9803436at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000051722; Unassembled WGS sequence.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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:SF4; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051722}.
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         51..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         252..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   SITE            162
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   351 AA;  38191 MW;  43D31C2B3B6E8A08 CRC64;
     MTSQNAPLQS VIWAEDRLDL LDQRLLPEEI VYLPLVTSED VWEAIRHLKV RGAPAIGISA
     AYGVVLGSRN ETTLKRWLEE VLNQAEYLAT SRPTAVNLFW ALDRMKARAE QLAAADLSLD
     EVKQALLNEA LAIHSEDEET NRLIGEHALT LFEDGMGVLT HCNAGGLATA KYGTALAPFY
     LALERGMSLR VFADETRPVL QGARLTAFEL QQAGVDVTLI CDNMAGMVMS KGWIQAVIVG
     TDRVAANGDV ANKIGTYSVA VLAKAHGIPV YVACPLSTID LNTPTGAEIP IEERSAEEIT
     EGFGKRTAPQ GVKVYNPAFD ITPNEYVTAI ITEKGIVQAP YDVNLKKLFN E
//
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