ID   RMGL_PICST              Reviewed;         336 AA.
AC   A3LZU8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=L-rhamnono-gamma-lactonase;
DE            EC=3.1.1.65;
GN   Name=LRA2; ORFNames=PICST_63908;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
RN   [2]
RP   CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, COFACTOR, AND
RP   IDENTIFICATION IN GENE CLUSTER.
RX   PubMed=18505728; DOI=10.1074/jbc.m801065200;
RA   Watanabe S., Saimura M., Makino K.;
RT   "Eukaryotic and bacterial gene clusters related to an alternative pathway
RT   of nonphosphorylated L-rhamnose metabolism.";
RL   J. Biol. Chem. 283:20372-20382(2008).
CC   -!- FUNCTION: Hydrolase with high substrate specificity for L-rhamnono-1,4-
CC       lactone. Catalyzes the second step in an alternative pathway for
CC       rhamnose utilization that does not involve phosphorylated
CC       intermediates. {ECO:0000269|PubMed:18505728}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-rhamnono-1,4-lactone = H(+) + L-rhamnonate;
CC         Xref=Rhea:RHEA:10288, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17937, ChEBI:CHEBI:58118; EC=3.1.1.65;
CC         Evidence={ECO:0000269|PubMed:18505728};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000305};
CC       Note=Divalent metal cation. {ECO:0000305};
CC   -!- ACTIVITY REGULATION: Inhibited by Zn(2+), Fe(2+) and Cu(2+), but not by
CC       EDTA. {ECO:0000269|PubMed:18505728}.
CC   -!- MISCELLANEOUS: Part of gene cluster that contains the genes for this
CC       rhamnose catabolic pathway.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000502; ABN68602.2; -; Genomic_DNA.
DR   RefSeq; XP_001386631.2; XM_001386594.1.
DR   AlphaFoldDB; A3LZU8; -.
DR   SMR; A3LZU8; -.
DR   STRING; 4924.XP_001386631.2; -.
DR   EnsemblFungi; ABN68602; ABN68602; PICST_63908.
DR   GeneID; 4840982; -.
DR   KEGG; pic:PICST_63908; -.
DR   eggNOG; ENOG502RZT7; Eukaryota.
DR   HOGENOM; CLU_044590_1_0_1; -.
DR   InParanoid; A3LZU8; -.
DR   OMA; HLCKPDF; -.
DR   OrthoDB; 1598530at2759; -.
DR   Proteomes; UP000002258; Chromosome 8.
DR   GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0050033; F:L-rhamnono-1,4-lactonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019301; P:rhamnose catabolic process; IDA:UniProtKB.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF04909; Amidohydro_2; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Reference proteome; Rhamnose metabolism.
FT   CHAIN           1..336
FT                   /note="L-rhamnono-gamma-lactonase"
FT                   /id="PRO_0000418399"
SQ   SEQUENCE   336 AA;  38836 MW;  4CFEDACA3A920D3C CRC64;
     MSKYKILDSH IHLYSLANIP LLHWDEGNPL HGNRRLDEYI ENSQSTQFDV EGVVWIECDA
     KIDLTQGLKG LENPIEEYLY ICRNINGKLL PEEGVSTPFK RRLIKAMIPF APMPLGSAGV
     EEYVKALKTR NSSEFHLVKG FRYLIQDKPP LTISDPHFVS SFQWLDSNGY VFDLGIDMRS
     GGLWQFKETL EVFKKVPNLK YIINHLTKPC LDFDPETIDS NPDFLSWKRL VTEMYITTPN
     SYMKLSGGFS EVEQDVALDV TSTSRHVYPW FKVVYELWGP ERTIFASNWP VCAIPAGQNL
     TEKWFQVCET LFDSIGMDED TRRKIYYSNA FKAYNI