(data stored in SCRATCH zone)

SWISSPROT: B1K8V5_BURCC

ID   B1K8V5_BURCC            Unreviewed;       371 AA.
AC   B1K8V5;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|PIRNR:PIRNR000183};
GN   OrderedLocusNames=Bcenmc03_3297 {ECO:0000313|EMBL:ACA92452.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92452.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000959; ACA92452.1; -; Genomic_DNA.
DR   RefSeq; WP_011547852.1; NC_010515.1.
DR   EnsemblBacteria; ACA92452; ACA92452; Bcenmc03_3297.
DR   KEGG; bcm:Bcenmc03_3297; -.
DR   HOGENOM; HOG000022120; -.
DR   KO; K00259; -.
DR   OMA; CFETSKA; -.
DR   BioCyc; BCEN406425:G1GBC-3502-MONOMER; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000002169; Chromosome 2.
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; B1K8V5.
DR   SWISS-2DPAGE; B1K8V5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
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}.
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}.
SQ   SEQUENCE   371 AA;  38353 MW;  8F33CBF3389EFB32 CRC64;
     MLIGVPKEIK NHEYRVGLTP AGARELTRHG HRVLVQRGAG TAIGLLDDDY TAAGASLGDG
     AEEIFARADM IIKVKEPQPT ECAMLRRGQI LYTYLHLAPD PDQAAALVKS GAVCIAYETV
     TGPGGGLPLL APMSEVAGRM SIQVAATHLE SPRGGRGLLM AGVPGVPAAH VVVLGAGVVG
     TGALQMAVGL GARVTVLDNN VNRLRQLDLV FANRIATVCS NAQTVDEAVR DADVVIGAVL
     VPGASAPRLV TRDMIATMRK GAVVVDVAID QGGCFETSHA TTHAAPTFVV DGVVHYCVAN
     MPGAVARTST FALNNATLGH ALALADKGWK QAMLDDPHLR AGLNVCDGHI TYEAVALALG
     LPYVPATGVL A
//

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