ID   GULDH_MYCTO             Reviewed;         428 AA.
AC   P9WIT2; 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=MT1821;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to L-xylo-hexulonolactone which
CC       spontaneously isomerizes to L-ascorbate. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Divalent metal cation. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46090.1; -; Genomic_DNA.
DR   PIR; D70989; D70989.
DR   RefSeq; WP_003408749.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIT2; -.
DR   SMR; P9WIT2; -.
DR   EnsemblBacteria; AAK46090; AAK46090; MT1821.
DR   KEGG; mtc:MT1821; -.
DR   PATRIC; fig|83331.31.peg.1960; -.
DR   HOGENOM; CLU_003896_4_3_11; -.
DR   UniPathway; UPA00132; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Ascorbate biosynthesis; Oxidoreductase.
FT   CHAIN           1..428
FT                   /note="L-gulono-1,4-lactone dehydrogenase"
FT                   /id="PRO_0000427950"
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