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Database: UniProt
Entry: A0A0K1PVR1_9DELT
LinkDB: A0A0K1PVR1_9DELT
Original site: A0A0K1PVR1_9DELT 
ID   A0A0K1PVR1_9DELT        Unreviewed;       370 AA.
AC   A0A0K1PVR1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   18-JUL-2018, entry version 16.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|PIRNR:PIRNR000183};
GN   ORFNames=AKJ09_04284 {ECO:0000313|EMBL:AKU97620.1};
OS   Labilithrix luteola.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Labilitrichaceae; Labilithrix.
OX   NCBI_TaxID=1391654 {ECO:0000313|EMBL:AKU97620.1, ECO:0000313|Proteomes:UP000064967};
RN   [1] {ECO:0000313|EMBL:AKU97620.1, ECO:0000313|Proteomes:UP000064967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27648 {ECO:0000313|EMBL:AKU97620.1,
RC   ECO:0000313|Proteomes:UP000064967};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3)
CC       + NADH. {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; CP012333; AKU97620.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKU97620; AKU97620; AKJ09_04284.
DR   KEGG; llu:AKJ09_04284; -.
DR   PATRIC; fig|1391654.3.peg.4343; -.
DR   KO; K00259; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000064967; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000064967};
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   Reference proteome {ECO:0000313|Proteomes:UP000064967}.
FT   DOMAIN        4    136       AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}.
FT   DOMAIN      148    296       AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}.
FT   NP_BIND     238    239       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   NP_BIND     266    269       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   NP_BIND     297    300       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   ACT_SITE     95     95       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   ACT_SITE    269    269       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   BINDING      15     15       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING      74     74       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING     133    133       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     197    197       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     219    219       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     278    278       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
SQ   SEQUENCE   370 AA;  38922 MW;  F68ACB28AF13328C CRC64;
     MIIGVPKEIK TREYRVGMTP AGVRSLTSRG HKVLVEKGAG EGAQIKDAEY VAQGATIVNT
     AAEAWGAEMV VKVKEPLPAE YGFFREGLIL YTYLHLAPEP ELTKQLAEKK VIGVAYETIE
     ADDGSLPLLR PMSEVAGRMA VQVGASALQK EHGGKGVLLG GVPGTRRGRV VILGGGIVGR
     NAATIAIGMG AQVTVLDVQA STMAYLEDIF GGAVETLYSN QTNIEQCVKN ADLVVGAVLV
     TGARAPKLVT EELVKQMQPG TVVVDVAVDQ GGCIETCRPT THDNPTYELH GVVHYCVANM
     PGAVAQTSTW ALTNTTIPYA VKIADLGIVA AAKADRALLK GINTYGGHVT CEPVAQAHKM
     EYVPAAKLLG
//
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