ID S5N3U2_SALBN Unreviewed; 354 AA. AC S5N3U2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 24-JUL-2024, entry version 51. DE RecName: Full=Probable L-ascorbate-6-phosphate lactonase UlaG {ECO:0000256|HAMAP-Rule:MF_01266}; DE EC=3.1.1.- {ECO:0000256|HAMAP-Rule:MF_01266}; DE AltName: Full=L-ascorbate utilization protein G {ECO:0000256|HAMAP-Rule:MF_01266}; GN Name=ulaG {ECO:0000256|HAMAP-Rule:MF_01266}; GN ORFNames=A464_4387 {ECO:0000313|EMBL:AGR61569.1}; OS Salmonella bongori N268-08. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1197719 {ECO:0000313|EMBL:AGR61569.1, ECO:0000313|Proteomes:UP000015042}; RN [1] {ECO:0000313|EMBL:AGR61569.1, ECO:0000313|Proteomes:UP000015042} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N268-08 {ECO:0000313|EMBL:AGR61569.1, RC ECO:0000313|Proteomes:UP000015042}; RA Marti R., Hagens S., Loessner M.J., Klumpp J.; RT "Genome sequence of Salmonella bongori N268-08 - a rare clinical isolate."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3- CC keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under CC anaerobic conditions. {ECO:0000256|HAMAP-Rule:MF_01266}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-ascorbate 6-phosphate = 3-dehydro-L-gulonate 6- CC phosphate; Xref=Rhea:RHEA:28803, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58774, ChEBI:CHEBI:61698; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01266}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01266}; CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5- CC phosphate from L-ascorbate: step 1/4. {ECO:0000256|HAMAP- CC Rule:MF_01266}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01266}. CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR. CC {ECO:0000256|HAMAP-Rule:MF_01266}. CC -!- SIMILARITY: Belongs to the UlaG family. {ECO:0000256|HAMAP- CC Rule:MF_01266}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP006608; AGR61569.1; -; Genomic_DNA. DR RefSeq; WP_000049161.1; NC_021870.1. DR AlphaFoldDB; S5N3U2; -. DR SMR; S5N3U2; -. DR GeneID; 66758606; -. DR KEGG; sbz:A464_4387; -. DR PATRIC; fig|1197719.3.peg.4380; -. DR eggNOG; COG2220; Bacteria. DR HOGENOM; CLU_074775_0_0_6; -. DR UniPathway; UPA00263; UER00377. DR Proteomes; UP000015042; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0035460; F:L-ascorbate 6-phosphate lactonase activity; IEA:InterPro. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd16284; UlaG-like_MBL-fold; 1. DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1. DR HAMAP; MF_01266; UlaG; 1. DR InterPro; IPR023951; L-ascorbate_6P_UlaG. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro. DR InterPro; IPR048021; UlaG-like_MBL-fold. DR InterPro; IPR050114; UPF0173_UPF0282_UlaG_hydrolase. DR PANTHER; PTHR43546:SF5; L-ASCORBATE-6-PHOSPHATE LACTONASE ULAG-RELATED; 1. DR PANTHER; PTHR43546; UPF0173 METAL-DEPENDENT HYDROLASE MJ1163-RELATED; 1. DR Pfam; PF12706; Lactamase_B_2; 1. DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1. PE 2: Evidence at transcript level; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01266}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01266}. FT DOMAIN 98..282 FT /note="Metallo-beta-lactamase" FT /evidence="ECO:0000259|Pfam:PF12706" SQ SEQUENCE 354 AA; 40073 MW; 556C9A927A2623D6 CRC64; MSKVQSITRE SWILSTFPEW GSWLNEEIEQ EQVAPGTFAM WWLGCTGIWL KSEGGTNVCV DFWCGTGKQS HGNPLMKTGH QMQRMAGVKK LQPNLRTTPF VLDPFAIRQI DAVLATHDHN DHIDVNVAAA VMQNCADDVP FIGPQTCVDL WVGWGVPKER CIVVKPGDVV KVKDIEIHAL DAFDRTALIT LPADQKAAGV LPDGMDVRAV NYLFKTPGGN LYHSGDSHYS NYYAKHGNEH QIDVALGSYG ENPRGITDKM TSADILRMAE SLNTKVVIPF HHDIWSNFQA DPQEIRVLWE MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL //