(data stored in ACNUC7421 zone)

SWISSPROT: A0KEW0_AERHH

ID   A0KEW0_AERHH            Unreviewed;       371 AA.
AC   A0KEW0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|PIRNR:PIRNR000183};
GN   Name=ald {ECO:0000313|EMBL:ABK36423.1};
GN   OrderedLocusNames=AHA_0248 {ECO:0000313|EMBL:ABK36423.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK36423.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK36423.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000183};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|PIRNR:PIRNR000183}.
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DR   EMBL; CP000462; ABK36423.1; -; Genomic_DNA.
DR   RefSeq; WP_011704256.1; NC_008570.1.
DR   RefSeq; YP_854776.1; NC_008570.1.
DR   STRING; 380703.AHA_0248; -.
DR   EnsemblBacteria; ABK36423; ABK36423; AHA_0248.
DR   GeneID; 4486949; -.
DR   KEGG; aha:AHA_0248; -.
DR   PATRIC; fig|380703.7.peg.235; -.
DR   eggNOG; ENOG4105DCF; Bacteria.
DR   eggNOG; COG0686; LUCA.
DR   HOGENOM; HOG000022120; -.
DR   KO; K00259; -.
DR   OMA; CFETSKA; -.
DR   BioCyc; AHYD380703:G1G7B-249-MONOMER; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05305; L-AlaDH; 1.
DR   InterPro; IPR008141; Ala_DH.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42795; PTHR42795; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF000183; Alanine_dh; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00518; alaDH; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KEW0.
DR   SWISS-2DPAGE; A0KEW0.
KW   NAD {ECO:0000256|PIRNR:PIRNR000183, ECO:0000256|PIRSR:PIRSR000183-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000183,
KW   ECO:0000313|EMBL:ABK36423.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN          4..137
FT                   /note="AlaDh_PNT_N"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          149..297
FT                   /note="AlaDh_PNT_C"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   NP_BIND         239..240
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   NP_BIND         267..270
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   NP_BIND         298..301
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   ACT_SITE        270
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   BINDING         15
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         75
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         134
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         198
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         203
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         220
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
SQ   SEQUENCE   371 AA;  38898 MW;  261F27C1A0EDAEDC CRC64;
     MIIGVPKEIK NHEYRVGMTP AGVQELTARG HKVLVQQQGG EAIGLSDAEY QAAGAELVAS
     AAEIFARAEM IVKVKEPQPE ECELLRPGQL LFTYLHLAPD PVQTQLLVHS GAVAIAYETV
     TDDRGGLPLL APMSEVAGRM AIQAGAHSLE KAQGGNGTLL GGVPAVAPAK VVVLGGGVVG
     VNSARMALGL GADVTILDRS LPRLRELDSL YGPALKTLYS TRTNIEACIA QADLVIGAVL
     IPGAAAPKLL TRDMLKLMRK GSVLVDVAID QGGCFETSHP TTHEEPTYVV DGIIHYCVAN
     MPGGVARTST FALTNATLPF VLALADKGYA RALQDDRHLR AGLNVFKGKI TQAAVAQALG
     YEYVSAESVL G
//

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