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Database: UniProt
Entry: A0A060JBW4_9MICO
LinkDB: A0A060JBW4_9MICO
Original site: A0A060JBW4_9MICO 
ID   A0A060JBW4_9MICO        Unreviewed;       372 AA.
AC   A0A060JBW4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   05-DEC-2018, entry version 23.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|PIRNR:PIRNR000183};
GN   ORFNames=Rhola_00005570 {ECO:0000313|EMBL:AIC47371.1};
OS   Rhodoluna lacicola.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Rhodoluna.
OX   NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC47371.1, ECO:0000313|Proteomes:UP000067708};
RN   [1] {ECO:0000313|EMBL:AIC47371.1, ECO:0000313|Proteomes:UP000067708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC47371.1,
RC   ECO:0000313|Proteomes:UP000067708};
RX   PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA   Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT   "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater
RT   bacterium with stream-lined genome.";
RL   Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57972;
CC         EC=1.4.1.1; 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
CC       1/1. {ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|PIRNR:PIRNR000183}.
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DR   EMBL; CP007490; AIC47371.1; -; Genomic_DNA.
DR   RefSeq; WP_038502198.1; NZ_CP007490.1.
DR   EnsemblBacteria; AIC47371; AIC47371; Rhola_00005570.
DR   KEGG; rla:Rhola_00005570; -.
DR   PATRIC; fig|529884.3.peg.532; -.
DR   KO; K00259; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000067708; 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; IPR008142; AlaDH/PNT_CS1.
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; PS00836; ALADH_PNT_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000067708};
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:AIC47371.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067708}.
FT   DOMAIN        4    137       AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}.
FT   DOMAIN      149    297       AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}.
FT   NP_BIND     239    240       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   NP_BIND     267    270       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   NP_BIND     298    301       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   ACT_SITE     96     96       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   ACT_SITE    270    270       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   BINDING      15     15       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING      75     75       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING     134    134       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     198    198       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     203    203       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     220    220       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     279    279       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
SQ   SEQUENCE   372 AA;  39451 MW;  D666D5E49C332929 CRC64;
     MRVGIPTEIK NNENRVAITP AGVHELVRRG HEVFIQVGAG LGSGFEDADY VAQGAKMLAT
     AAEVWAAGDL LLKVKEPIKA EYELMRRDQV LFTYLHLAAS RECTDALIAA GTTAIAYETV
     QLPNRALPLL QPMSEVAGRL SAQIGAYQLM KNEGGRGVLM GGVPGAPKAK VVVIGGGVAG
     EHAATMALGM QAEVTVIDIS LPKLRELDAR FGGHVRTRVS TALEIAEQLK DADLVIGSVL
     IPGEKAPKLV TDEMVKNMKP GSVLVDIAID QGGCFENSRA TTHDDPTYMV HNSIYYCVAN
     MPGAVPATST RALTNATLPY VIALADKGWK AALAADESLA KGLNVHDGKV TYSGVLHAFP
     ELPFQDLHEA IA
//
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