ID A0A0R0D8C4_9GAMM Unreviewed; 353 AA.
AC A0A0R0D8C4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=ABB28_10595 {ECO:0000313|EMBL:KRG73480.1};
OS Stenotrophomonas chelatiphaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG73480.1, ECO:0000313|Proteomes:UP000051386};
RN [1] {ECO:0000313|EMBL:KRG73480.1, ECO:0000313|Proteomes:UP000051386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG73480.1,
RC ECO:0000313|Proteomes:UP000051386};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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:KRG73480.1}.
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DR EMBL; LDJK01000044; KRG73480.1; -; Genomic_DNA.
DR RefSeq; WP_057508595.1; NZ_LDJK01000044.1.
DR AlphaFoldDB; A0A0R0D8C4; -.
DR PATRIC; fig|517011.3.peg.1831; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000051386; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051386}.
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 255..256
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 165
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 353 AA; 37106 MW; 06C59F9FEFD471E9 CRC64;
MNTPTEIDYA RYDHIRPILW TGDALQLLDQ RKLPFVVEHV ACTTSDEVAS AIHALTVRGA
PAIGIAAAWG VVLAARDVQA EDGPQALQKL EPALQRLNAS RPTAVNLAWA LARMRRVLAA
AGADWSAVLE REAEAIATED LAANRHMGAL GAGLIDAGSG VLTHCNTGSL ATAGFGTALG
VIRAGMAQQR IAKVFAGETR PWLQGARLTV WELQQDGIDA TLIADSAASH LMKTGAVQWV
IVGADRICAN GDTANKIGTY QLAIAARHHG VKFMVVAPSS TVDMDTADGS EIEIEQRDPG
ELYGVGGSRT VADGIAAWNP VFDVTPGELI DAIVTERGVI LAPTVANMRA AFG
//
