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L-arabinose 1-dehydrogenase (NAD(P)( )) (EC 1.1.1.376) (D-galactose 1-dehydrogenase) (EC 1.1.1.120) (EC 1.1.1.48)

 ARAA_AZOBR              Reviewed;         309 AA.
Q53TZ2;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
10-MAY-2017, entry version 44.
RecName: Full=L-arabinose 1-dehydrogenase (NAD(P)(+)) {ECO:0000303|PubMed:16326697};
EC=1.1.1.376 {ECO:0000269|PubMed:16326697};
AltName: Full=D-galactose 1-dehydrogenase {ECO:0000303|PubMed:16326697};
EC=1.1.1.120 {ECO:0000269|PubMed:16326697};
EC=1.1.1.48 {ECO:0000269|PubMed:16326697};
Name=araA;
Azospirillum brasilense.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
Rhodospirillaceae; Azospirillum.
NCBI_TaxID=192;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16 AND
89-103, FUNCTION IN ARABINOSE DEGRADATION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
SUBUNIT, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-169 AND ASN-173,
REACTION MECHANISM, PATHWAY, AND ACTIVE SITE.
STRAIN=ATCC 29145 / Sp7 / DSM 1690 / IMET 11303;
PubMed=16326697; DOI=10.1074/jbc.M506477200;
Watanabe S., Kodaki T., Makino K.;
"Cloning, expression, and characterization of bacterial L-arabinose 1-
dehydrogenase involved in an alternative pathway of L-arabinose
metabolism.";
J. Biol. Chem. 281:2612-2623(2006).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 29145 / Sp7 / DSM 1690 / IMET 11303;
PubMed=16950779; DOI=10.1074/jbc.M606727200;
Watanabe S., Shimada N., Tajima K., Kodaki T., Makino K.;
"Identification and characterization of L-arabonate dehydratase, L-2-
keto-3-deoxyarabonate dehydratase and L-arabinolactonase involved in
an alternative pathway of L-arabinose metabolism: novel evolutionary
insight into sugar metabolism.";
J. Biol. Chem. 281:33521-33536(2006).
[3]
PATHWAY.
STRAIN=ATCC 29145 / Sp7 / DSM 1690 / IMET 11303;
PubMed=6798025;
Novick N.J., Tyler M.E.;
"L-arabinose metabolism in Azospirillum brasiliense.";
J. Bacteriol. 149:364-367(1982).
-!- FUNCTION: Catalyzes the NAD(P)(+)-dependent conversion of L-
arabinose to L-arabino-gamma-lactone. Is involved in a degradation
pathway of L-arabinose that allows A.brasilense to grow on L-
arabinose as a sole carbon source. Prefers NADP(+) to NAD(+) as
electron acceptor. Displays high catalytic efficiency for both L-
arabinose and D-galactose in vitro. However, the enzyme appears to
be involved in the metabolism of L-arabinose but not D-galactose
in vivo. To a lesser extent, is also active on D-talose and D-
xylose as substrates in vitro, but not with D-arabinose, D-
glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-fructose.
{ECO:0000269|PubMed:16326697}.
-!- CATALYTIC ACTIVITY: L-arabinose + NAD(P)(+) = L-arabinono-1,4-
lactone + NAD(P)H. {ECO:0000269|PubMed:16326697}.
-!- CATALYTIC ACTIVITY: D-galactose + NAD(+) = D-galactono-1,4-lactone
+ NADH. {ECO:0000269|PubMed:16326697}.
-!- CATALYTIC ACTIVITY: D-galactose + NADP(+) = D-galactono-1,5-
lactone + NADPH. {ECO:0000269|PubMed:16326697}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.41 mM for L-arabinose (in the presence of NAD(+), at 30
degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=0.255 mM for L-arabinose (in the presence of NADP(+), at 30
degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=1.49 mM for D-galactose (in the presence of NAD(+), at 30
degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=0.109 mM for D-galactose (in the presence of NADP(+), at 30
degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=3.95 mM for D-talose (in the presence of NAD(+), at 30
degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=5.87 mM for D-talose (in the presence of NADP(+), at 30
degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=210 mM for D-xylose (in the presence of NAD(+), at 30 degrees
Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=72.0 mM for D-xylose (in the presence of NADP(+), at 30
degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
KM=0.0095 mM for NADP(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
KM=0.053 mM for NAD(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=25.0 umol/min/mg enzyme for the L-arabinose oxidation with
NAD(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=44.9 umol/min/mg enzyme for the L-arabinose oxidation with
NADP(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=23.8 umol/min/mg enzyme for the D-galactose oxidation with
NAD(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=35.6 umol/min/mg enzyme for the D-galactose oxidation with
NADP(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=1.7 umol/min/mg enzyme for the D-talose oxidation with
NAD(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=12.8 umol/min/mg enzyme for the D-talose oxidation with
NADP(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=5.3 umol/min/mg enzyme for the D-xylose oxidation with
NAD(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
Vmax=14.8 umol/min/mg enzyme for the D-xylose oxidation with
NADP(+) (at 30 degrees Celsius and pH 9.0)
{ECO:0000269|PubMed:16326697};
-!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
arabinono-1,4-lactone pathway. {ECO:0000305|PubMed:16326697}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16326697}.
-!- INDUCTION: Induced by L-arabinose but not by D-galactose, D-xylose
and D-glucose. {ECO:0000269|PubMed:16326697}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow on L-
arabinose as a sole carbon source but grow on D-galactose, D-
xylose or D-glucose at the same growth rate as the wild-type
strain. {ECO:0000269|PubMed:16326697}.
-!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB211983; BAD95974.1; -; Genomic_DNA.
EMBL; AB241136; BAE94271.1; -; Genomic_DNA.
ProteinModelPortal; Q53TZ2; -.
SMR; Q53TZ2; -.
KEGG; ag:BAD95974; -.
KO; K13873; -.
BRENDA; 1.1.1.376; 611.
UniPathway; UPA00141; -.
GO; GO:0047910; F:galactose 1-dehydrogenase (NADP+) activity; IDA:UniProtKB.
GO; GO:0019151; F:galactose 1-dehydrogenase activity; IDA:UniProtKB.
GO; GO:0050022; F:L-arabinose 1-dehydrogenase (NAD+) activity; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0019572; P:L-arabinose catabolic process; IMP:UniProtKB.
GO; GO:0019570; P:L-arabinose catabolic process to 2-oxoglutarate; IDA:UniProtKB.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR000683; Oxidoreductase_N.
Pfam; PF01408; GFO_IDH_MocA; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Arabinose catabolism; Carbohydrate metabolism;
Direct protein sequencing; NAD; NADP; Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:16326697}.
CHAIN 2 309 L-arabinose 1-dehydrogenase (NAD(P)(+)).
/FTId=PRO_0000418504.
ACT_SITE 169 169 Proton acceptor.
{ECO:0000305|PubMed:16326697}.
MUTAGEN 169 169 D->A: Loss of activity.
{ECO:0000269|PubMed:16326697}.
MUTAGEN 173 173 N->A: Decrease by 4 orders of magnitude
in catalytic efficiency.
{ECO:0000269|PubMed:16326697}.
SEQUENCE 309 AA; 33796 MW; 480C99414F82BDC2 CRC64;
MSDQVSLGVV GIGKIARDQH LPAIDAEPGF KLTACASRHA EVTGVRNYRD LRALLAAERE
LDAVSLCAPP QVRYAQARAA LEAGKHVMLE KPPGATLGEV AVLEALARER GLTLFATWHS
RCASAVEPAR EWLATRAIRA VQVRWKEDVR RWHPGQQWIW EPGGLGVFDP GINALSIVTR
ILPRELVLRE ATLIVPSDVQ TPIAAELDCA DTDGVPVRAE FDWRHGPVEQ WEIAVDTADG
VLAISRGGAQ LSIAGEPVEL GPEREYPALY AHFHALIARG ESDVDVRPLR LVADAFLFGR
RVQTDAFGR


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