ID   GLCAL_PSEFL             Reviewed;         320 AA.
AC   Q93HX6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Glucosaminate ammonia-lyase;
DE            EC=4.3.1.9 {ECO:0000269|PubMed:12686150};
DE   AltName: Full=D-glucosaminate dehydratase alpha-subunit;
DE   AltName: Full=GlcNA-DH alpha subunit;
DE            Short=GlcNADH-alpha;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 119-131; 225-234;
RP   259-282 AND 311-320, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=12686150; DOI=10.1016/s1570-9639(03)00079-7;
RA   Iwamoto R., Amano C., Ikehara K., Ushida N.;
RT   "The D-glucosaminate dehydratase alpha-subunit from Pseudomonas fluorescens
RT   exhibits thioredoxin reductase activity.";
RL   Biochim. Biophys. Acta 1647:310-314(2003).
CC   -!- FUNCTION: Catalyzes the conversion of 2-amino-2-deoxy-D-gluconate
CC       (GlcNA) to 2-keto-3-deoxy-D-gluconic acid (KDGA) and ammonia.
CC       {ECO:0000269|PubMed:12686150}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate +
CC         NH4(+); Xref=Rhea:RHEA:12488, ChEBI:CHEBI:28938, ChEBI:CHEBI:57990,
CC         ChEBI:CHEBI:58269; EC=4.3.1.9;
CC         Evidence={ECO:0000269|PubMed:12686150};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.4 uM for Thioredoxin {ECO:0000269|PubMed:12686150};
CC         KM=11.3 uM for NADPH {ECO:0000269|PubMed:12686150};
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB64360.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB64360.1; Type=Miscellaneous discrepancy; Note=The sequence does not corresponds to the one published in PubMed:12686150.; Evidence={ECO:0000305};
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DR   EMBL; AB053183; BAB64360.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q93HX6; -.
DR   SMR; Q93HX6; -.
DR   STRING; 690597.JH730972_gene2176; -.
DR   PRIDE; Q93HX6; -.
DR   eggNOG; COG0492; Bacteria.
DR   BRENDA; 4.3.1.9; 5121.
DR   SABIO-RK; Q93HX6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0047930; F:glucosaminate ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Lyase;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN           1..320
FT                   /note="Glucosaminate ammonia-lyase"
FT                   /id="PRO_0000419105"
FT   BINDING         36..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         285..294
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        136..139
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  33907 MW;  4AF2A9E0F3DBD50B CRC64;
     MVEVRHSRVI ILGSGPAGYS AAVYAARANL KPLLITGMQA GGQLTTTTEV DNWPGDVHGL
     TGPALMERMR EHAERFETEI VFDHINAVDF AAKPYTLTGD SATYTCDALI IATGASARYL
     GLPSEEAFMG KGVSACATCD GFFYRNKPVA VVGGGNTAVE EALYLANIAS TVTLIHRRET
     FRAEKILIDK LNARVAEGKI ILKLNANLDE VLGDNMGVTG ARLKNNDGSF DELKVDGVFI
     AIGHTPNTSL FEGQLTLKDG YLVVQGGRDG NATATSVEGI FAAGDVADHV YRQAITSAGA
     GCMAALDTER YLDGLQNASE