ID S5N3U2_SALBN Unreviewed; 354 AA. AC S5N3U2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 15-MAR-2017, entry version 27. 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; Proteobacteria; 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 RT isolate."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probably catalyzes the hydrolysis of L-ascorbate-6-P CC into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate CC utilization under anaerobic conditions. {ECO:0000256|HAMAP- CC Rule:MF_01266}. CC -!- CATALYTIC ACTIVITY: L-ascorbate 6-phosphate + H(2)O = 3-dehydro-L- CC gulonate 6-phosphate. {ECO:0000256|HAMAP-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 CC 5-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 ProteinModelPortal; S5N3U2; -. DR SMR; S5N3U2; -. DR EnsemblBacteria; AGR61569; AGR61569; A464_4387. DR KEGG; sbz:A464_4387; -. DR KO; K03476; -. DR OrthoDB; POG091H066N; -. 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-HAMAP. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_01266; UlaG; 1. DR InterPro; IPR023951; L-ascorbate_6P_UlaG. DR InterPro; IPR001279; Metallo-B-lactamas. DR SUPFAM; SSF56281; SSF56281; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000015042}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01266}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01266}. 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 //