ID   GULDH_MYCTU             Reviewed;         428 AA.
AC   P9WIT3; F2GJF7; L0TAK3; O06804; Q7D7Z8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=L-gulono-1,4-lactone dehydrogenase;
DE            EC=1.1.2.-;
GN   OrderedLocusNames=Rv1771;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ABSENCE OF
RP   FAD-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP   PATHWAY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16956367; DOI=10.1111/j.1742-4658.2006.05443.x;
RA   Wolucka B.A., Communi D.;
RT   "Mycobacterium tuberculosis possesses a functional enzyme for the synthesis
RT   of vitamin C, L-gulono-1,4-lactone dehydrogenase.";
RL   FEBS J. 273:4435-4445(2006).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to L-xylo-hexulonolactone which
CC       spontaneously isomerizes to L-ascorbate. Can use both cytochrome c and
CC       phenazine methosulfate as exogenous electron acceptors, but molecular
CC       oxygen does not serve as a substrate. Is very specific for the L-
CC       gulono-1,4-lactone substrate, since it cannot oxidize L-galactono-1,4-
CC       lactone, D-glucurono-3,6-lactone, D-glucuronate, D-arabinose, or D-
CC       xylose. {ECO:0000269|PubMed:16956367}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome c] + L-gulono-1,4-lactone = 2 Fe(II)-
CC         [cytochrome c] + 3 H(+) + L-ascorbate; Xref=Rhea:RHEA:47248,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17587, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:16956367};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000305|PubMed:16956367};
CC       Note=Divalent metal cation. {ECO:0000305|PubMed:16956367};
CC   -!- ACTIVITY REGULATION: Is completely inhibited by EDTA, N-ethylmaleimide,
CC       Cu(2+), Zn(2+), and potassium cyanide in vitro. Mg(2+) and Ca(2+) have
CC       no effect on the dehydrogenase activity, and 1 mm Mn(2+) slightly
CC       inhibit the enzyme (21% inhibition). {ECO:0000269|PubMed:16956367}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.5 mM for L-gulono-1,4-lactone {ECO:0000269|PubMed:16956367};
CC         KM=4.7 uM for ferricytochrome c {ECO:0000269|PubMed:16956367};
CC         Vmax=2.44 umol/h/mg enzyme {ECO:0000269|PubMed:16956367};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:16956367};
CC       Temperature dependence:
CC         Optimum temperature is 39 degrees Celsius. Is relatively thermostable
CC         since preincubation at 60 degrees Celsius for 5 minutes results in
CC         only partial inactivation of the enzyme (53% of control).
CC         {ECO:0000269|PubMed:16956367};
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC       {ECO:0000269|PubMed:16956367}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to mammalian L-gulono-1,4-lactone oxidases, the
CC       ortholog in M.tuberculosis is not a flavoenzyme. {ECO:0000305}.
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; AL123456; CCP44538.1; -; Genomic_DNA.
DR   PIR; D70989; D70989.
DR   RefSeq; NP_216287.1; NC_000962.3.
DR   RefSeq; WP_003408749.1; NZ_NVQJ01000037.1.
DR   AlphaFoldDB; P9WIT3; -.
DR   SMR; P9WIT3; -.
DR   STRING; 83332.Rv1771; -.
DR   PaxDb; P9WIT3; -.
DR   DNASU; 885441; -.
DR   GeneID; 885441; -.
DR   KEGG; mtu:Rv1771; -.
DR   PATRIC; fig|83332.12.peg.1978; -.
DR   TubercuList; Rv1771; -.
DR   eggNOG; COG0277; Bacteria.
DR   OMA; YPRFGEF; -.
DR   PhylomeDB; P9WIT3; -.
DR   BioCyc; MetaCyc:G185E-5967-MON; -.
DR   UniPathway; UPA00132; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0080049; F:L-gulono-1,4-lactone dehydrogenase activity; IDA:MTBBASE.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IDA:MTBBASE.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR007173; ALO_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR010031; FAD_lactone_oxidase.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR43762; PTHR43762; 1.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PIRSF; PIRSF000136; LGO_GLO; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   1: Evidence at protein level;
KW   Ascorbate biosynthesis; Oxidoreductase; Reference proteome.
FT   CHAIN           1..428
FT                   /note="L-gulono-1,4-lactone dehydrogenase"
FT                   /id="PRO_0000420410"
FT   DOMAIN          12..179
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   428 AA;  48045 MW;  F1CC666F3B15A50B CRC64;
     MSPIWSNWPG EQVCAPSAIV RPTSEAELAD VIAQAAKRGE RVRAVGSGHS FTDIACTDGV
     MIDMTGLQRV LDVDQPTGLV TVEGGAKLRA LGPQLAQRRL GLENQGDVDP QSITGATATA
     THGTGVRFQN LSARIVSLRL VTAGGEVLSL SEGDDYLAAR VSLGALGVIS QVTLQTVPLF
     TLHRHDQRRS LAQTLERLDE FVDGNDHFEF FVFPYADKAL TRTMHRSDEQ PKPTPGWQRM
     VGENFENGGL SLICQTGRRF PSVAPRLNRL MTNMMSSSTV QDRAYKVFAT QRKVRFTEME
     YAIPRENGRE ALQRVIDLVR RRSLPIMFPI EVRFSAPDDS FLSTAYGRDT CYIAVHQYAG
     MEFESYFRAV EEIMDDYAGR PHWGKRHYQT AATLRERYPQ WDRFAAVRDR LDPDRVFLND
     YTRRVLGP