(data stored in ACNUC10043 zone)

SWISSPROT: D1YVC7_METPS

ID   D1YVC7_METPS            Unreviewed;       325 AA.
AC   D1YVC7;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 55.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00935};
DE            Short=AlaDH {ECO:0000256|HAMAP-Rule:MF_00935};
DE            EC=1.4.1.1 {ECO:0000256|HAMAP-Rule:MF_00935};
GN   Name=ala {ECO:0000256|HAMAP-Rule:MF_00935};
GN   OrderedLocusNames=MCP_0327 {ECO:0000313|EMBL:BAI60399.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60399.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidative deamination of L-
CC       alanine to pyruvate, and the reverse reaction, the reductive amination
CC       of pyruvate. {ECO:0000256|HAMAP-Rule:MF_00935}.
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|HAMAP-Rule:MF_00935};
CC   -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC       family. Archaeal alanine dehydrogenase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00935}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00935}.
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DR   EMBL; AP011532; BAI60399.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0327; -.
DR   EnsemblBacteria; BAI60399; BAI60399; MCP_0327.
DR   KEGG; mpd:MCP_0327; -.
DR   PATRIC; fig|304371.9.peg.333; -.
DR   eggNOG; arCOG01035; Archaea.
DR   eggNOG; COG2423; LUCA.
DR   HOGENOM; HOG000137263; -.
DR   KO; K19244; -.
DR   OMA; HTHINAM; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1780.10; -; 1.
DR   HAMAP; MF_00935; AlaDH_arch; 1.
DR   InterPro; IPR012742; Ala_DH_archaeglobus.
DR   InterPro; IPR028609; AlaDH_arch-typ.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   InterPro; IPR023401; ODC_N.
DR   PANTHER; PTHR13812; PTHR13812; 1.
DR   Pfam; PF02423; OCD_Mu_crystall; 1.
DR   PIRSF; PIRSF001439; CryM; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR02371; ala_DH_arch; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVC7.
DR   SWISS-2DPAGE; D1YVC7.
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00935};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00935};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00935};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   NP_BIND         137..138
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   NP_BIND         223..225
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   ACT_SITE        67
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         110
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         229
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         296
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ   SEQUENCE   325 AA;  35086 MW;  2E11B7BC36646E59 CRC64;
     MVRLLSDTDI KRLVTMNDIV PAVENVFAEY AEGRVEMPSK IYLDIKGYGD FRAMPSYVPS
     IGTAGVKWVN VHPDNPSKGL PTVMATILLN DPETGRLICV MNGSTLTDER TGAAGGVAAK
     YLARKDSSVV GLIGSGHQAY TQMLAYNVVF GRQIKLVKVY SRHPEHAEAL AGRIRAEMGY
     DAQAVMTAQE AADSDIIATI TPARRPVLIA DWVKPGTHIN AIGADAPGKQ ELESMLTVKA
     RVFVDSVEQA SHSGEINVPW SQGLLNKDKL AGTIGEVIVG MMPGRTSDRE ITVFDSTGLS
     IQDMAVAHLV YERALKEHIG TDVNI
//

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