ARAA_AZOBR
ID ARAA_AZOBR Reviewed; 309 AA.
AC Q53TZ2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=L-arabinose 1-dehydrogenase (NAD(P)(+)) {ECO:0000303|PubMed:16326697};
DE EC=1.1.1.376 {ECO:0000269|PubMed:16326697};
DE AltName: Full=D-galactose 1-dehydrogenase {ECO:0000303|PubMed:16326697};
DE EC=1.1.1.120 {ECO:0000269|PubMed:16326697};
DE EC=1.1.1.48 {ECO:0000269|PubMed:16326697};
GN Name=araA;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16 AND 89-103,
RP FUNCTION IN ARABINOSE DEGRADATION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBUNIT, DISRUPTION
RP PHENOTYPE, MUTAGENESIS OF ASP-169 AND ASN-173, REACTION MECHANISM, AND
RP PATHWAY.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=16326697; DOI=10.1074/jbc.m506477200;
RA Watanabe S., Kodaki T., Makino K.;
RT "Cloning, expression, and characterization of bacterial L-arabinose 1-
RT dehydrogenase involved in an alternative pathway of L-arabinose
RT metabolism.";
RL J. Biol. Chem. 281:2612-2623(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=16950779; DOI=10.1074/jbc.m606727200;
RA Watanabe S., Shimada N., Tajima K., Kodaki T., Makino K.;
RT "Identification and characterization of L-arabonate dehydratase, L-2-keto-
RT 3-deoxyarabonate dehydratase and L-arabinolactonase involved in an
RT alternative pathway of L-arabinose metabolism: novel evolutionary insight
RT into sugar metabolism.";
RL J. Biol. Chem. 281:33521-33536(2006).
RN [3]
RP PATHWAY.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=6798025; DOI=10.1128/jb.149.1.364-367.1982;
RA Novick N.J., Tyler M.E.;
RT "L-arabinose metabolism in Azospirillum brasiliense.";
RL J. Bacteriol. 149:364-367(1982).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent conversion of L-arabinose
CC to L-arabino-gamma-lactone. Is involved in a degradation pathway of L-
CC arabinose that allows A.brasilense to grow on L-arabinose as a sole
CC carbon source. Prefers NADP(+) to NAD(+) as electron acceptor. Displays
CC high catalytic efficiency for both L-arabinose and D-galactose in
CC vitro. However, the enzyme appears to be involved in the metabolism of
CC L-arabinose but not D-galactose in vivo. To a lesser extent, is also
CC active on D-talose and D-xylose as substrates in vitro, but not with D-
CC arabinose, D-glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-
CC fructose. {ECO:0000269|PubMed:16326697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-
CC lactone + NADH; Xref=Rhea:RHEA:17925, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17100, ChEBI:CHEBI:46987, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.376;
CC Evidence={ECO:0000269|PubMed:16326697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-arabinopyanose + NADP(+) = H(+) + L-arabinono-1,4-
CC lactone + NADPH; Xref=Rhea:RHEA:42664, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17100, ChEBI:CHEBI:46987, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.376;
CC Evidence={ECO:0000269|PubMed:16326697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:21296, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15895, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.48;
CC Evidence={ECO:0000269|PubMed:16326697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) +
CC NADPH; Xref=Rhea:RHEA:18625, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15945, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.120; Evidence={ECO:0000269|PubMed:16326697};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.41 mM for L-arabinose (in the presence of NAD(+), at 30 degrees
CC Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=0.255 mM for L-arabinose (in the presence of NADP(+), at 30
CC degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=1.49 mM for D-galactose (in the presence of NAD(+), at 30 degrees
CC Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=0.109 mM for D-galactose (in the presence of NADP(+), at 30
CC degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=3.95 mM for D-talose (in the presence of NAD(+), at 30 degrees
CC Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=5.87 mM for D-talose (in the presence of NADP(+), at 30 degrees
CC Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=210 mM for D-xylose (in the presence of NAD(+), at 30 degrees
CC Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=72.0 mM for D-xylose (in the presence of NADP(+), at 30 degrees
CC Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC KM=0.0095 mM for NADP(+) (at 30 degrees Celsius and pH 9.0)
CC {ECO:0000269|PubMed:16326697};
CC KM=0.053 mM for NAD(+) (at 30 degrees Celsius and pH 9.0)
CC {ECO:0000269|PubMed:16326697};
CC Vmax=25.0 umol/min/mg enzyme for the L-arabinose oxidation with
CC NAD(+) (at 30 degrees Celsius and pH 9.0)
CC {ECO:0000269|PubMed:16326697};
CC Vmax=44.9 umol/min/mg enzyme for the L-arabinose oxidation with
CC NADP(+) (at 30 degrees Celsius and pH 9.0)
CC {ECO:0000269|PubMed:16326697};
CC Vmax=23.8 umol/min/mg enzyme for the D-galactose oxidation with
CC NAD(+) (at 30 degrees Celsius and pH 9.0)
CC {ECO:0000269|PubMed:16326697};
CC Vmax=35.6 umol/min/mg enzyme for the D-galactose oxidation with
CC NADP(+) (at 30 degrees Celsius and pH 9.0)
CC {ECO:0000269|PubMed:16326697};
CC Vmax=1.7 umol/min/mg enzyme for the D-talose oxidation with NAD(+)
CC (at 30 degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC Vmax=12.8 umol/min/mg enzyme for the D-talose oxidation with NADP(+)
CC (at 30 degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC Vmax=5.3 umol/min/mg enzyme for the D-xylose oxidation with NAD(+)
CC (at 30 degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC Vmax=14.8 umol/min/mg enzyme for the D-xylose oxidation with NADP(+)
CC (at 30 degrees Celsius and pH 9.0) {ECO:0000269|PubMed:16326697};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC arabinono-1,4-lactone pathway. {ECO:0000305|PubMed:16326697}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16326697}.
CC -!- INDUCTION: Induced by L-arabinose but not by D-galactose, D-xylose and
CC D-glucose. {ECO:0000269|PubMed:16326697}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow on L-
CC arabinose as a sole carbon source but grow on D-galactose, D-xylose or
CC D-glucose at the same growth rate as the wild-type strain.
CC {ECO:0000269|PubMed:16326697}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AB211983; BAD95974.1; -; Genomic_DNA.
DR EMBL; AB241136; BAE94271.1; -; Genomic_DNA.
DR PDB; 6JNJ; X-ray; 1.50 A; A/B=1-309.
DR PDB; 6JNK; X-ray; 2.20 A; A/B/C/D=2-309.
DR PDB; 7CGQ; X-ray; 2.21 A; A/B/C/D=2-309.
DR PDB; 7CGR; X-ray; 2.09 A; A/B/C/D=2-309.
DR PDBsum; 6JNJ; -.
DR PDBsum; 6JNK; -.
DR PDBsum; 7CGQ; -.
DR PDBsum; 7CGR; -.
DR AlphaFoldDB; Q53TZ2; -.
DR SMR; Q53TZ2; -.
DR KEGG; ag:BAD95974; -.
DR BRENDA; 1.1.1.376; 611.
DR SABIO-RK; Q53TZ2; -.
DR UniPathway; UPA00141; -.
DR GO; GO:0047910; F:galactose 1-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0019151; F:galactose 1-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0050022; F:L-arabinose 1-dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0044103; F:L-arabinose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0019572; P:L-arabinose catabolic process; IMP:UniProtKB.
DR GO; GO:0019570; P:L-arabinose catabolic process to 2-oxoglutarate; IDA:UniProtKB.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arabinose catabolism; Carbohydrate metabolism;
KW Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16326697"
FT CHAIN 2..309
FT /note="L-arabinose 1-dehydrogenase (NAD(P)(+))"
FT /id="PRO_0000418504"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8,
FT ECO:0000305|PubMed:16326697"
FT MUTAGEN 169
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16326697"
FT MUTAGEN 173
FT /note="N->A: Decrease by 4 orders of magnitude in catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:16326697"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7CGR"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7CGR"
FT HELIX 265..279
FT /evidence="ECO:0007829|PDB:6JNJ"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:6JNJ"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:6JNJ"
SQ 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
