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Database: UniProt
Entry: A0A0L0KPU7_9ACTN
LinkDB: A0A0L0KPU7_9ACTN
Original site: A0A0L0KPU7_9ACTN 
ID   A0A0L0KPU7_9ACTN        Unreviewed;       374 AA.
AC   A0A0L0KPU7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   10-OCT-2018, entry version 18.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|PIRNR:PIRNR000183};
GN   ORFNames=IQ63_01525 {ECO:0000313|EMBL:KND39866.1};
OS   Streptomyces acidiscabies.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=42234 {ECO:0000313|EMBL:KND39866.1, ECO:0000313|Proteomes:UP000037151};
RN   [1] {ECO:0000313|Proteomes:UP000037151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA   Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT   "Genome sequencing of plant-pathogenic Streptomyces species.";
RL   Submitted (JUL-2014) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000183-4};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000183-4};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KND39866.1}.
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DR   EMBL; JPPY01000014; KND39866.1; -; Genomic_DNA.
DR   RefSeq; WP_050369029.1; NZ_KQ257795.1.
DR   EnsemblBacteria; KND39866; KND39866; IQ63_01525.
DR   PATRIC; fig|42234.21.peg.322; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000037151; Unassembled WGS sequence.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UP000037151};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000183-4};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000183-4};
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:UP000037151}.
FT   DOMAIN        7    140       AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}.
FT   DOMAIN      152    300       AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}.
FT   NP_BIND     242    243       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   NP_BIND     270    273       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   NP_BIND     301    304       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   ACT_SITE     99     99       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   ACT_SITE    273    273       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000183-1}.
FT   METAL       326    326       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000183-4}.
FT   METAL       330    330       Magnesium; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000183-4}.
FT   BINDING      18     18       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING      78     78       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000183-2}.
FT   BINDING     137    137       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     201    201       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     206    206       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     223    223       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
FT   BINDING     282    282       NAD. {ECO:0000256|PIRSR:PIRSR000183-3}.
SQ   SEQUENCE   374 AA;  39694 MW;  D3B9DEF0B6360816 CRC64;
     MIDVKVGIPR EVKNNEFRVA ITPAGVHELV RHGHEVVIER GAGVGSSIPD EEYVAAGAAI
     LETADEVWGA ADLLLKVKEP VAEEYHRLRK DQTLFTYLHL AASKECTDAL VASGTTAIAY
     ETVELPGRAL PLLAPMSEVA GRLAPQVGAY HLMRSAGGRG VLPGGVPGTQ PAKAVVIGGG
     VSGWNATQIA IGLGFHVTLL DRDIHKLREA DKVFGTRVRA IMSNSFELEK AVLDADLVVG
     AVLIPGAKAP KLVTNELVAR MKPGSVLVDI AIDQGGCFED SRPTTHAEPT FAVHESVFYC
     VANMPGAVPN TSTYALTNAT LPYIVELADH GWAEALRRDP ALAKGLNTHD GKVVYREVAE
     AHGLEHVELT SLLG
//
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