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Database: UniProt
Entry: K8Z8A0_9ENTE
LinkDB: K8Z8A0_9ENTE
Original site: K8Z8A0_9ENTE 
ID   K8Z8A0_9ENTE            Unreviewed;       365 AA.
AC   K8Z8A0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183};
GN   ORFNames=C683_0600 {ECO:0000313|EMBL:EKU27269.1};
OS   Catellicoccus marimammalium M35/04/3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Catellicoccus.
OX   NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU27269.1, ECO:0000313|Proteomes:UP000016057};
RN   [1] {ECO:0000313|EMBL:EKU27269.1, ECO:0000313|Proteomes:UP000016057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU27269.1,
RC   ECO:0000313|Proteomes:UP000016057};
RX   PubMed=23405330;
RA   Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., Santo Domingo J.W.;
RT   "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT   Commonly Found in Gull Feces.";
RL   Genome Announc. 1:E00019-12(2013).
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|PIRNR:PIRNR000183};
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKU27269.1}.
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DR   EMBL; AMYT01000017; EKU27269.1; -; Genomic_DNA.
DR   RefSeq; WP_009489875.1; NZ_AMYT01000017.1.
DR   AlphaFoldDB; K8Z8A0; -.
DR   STRING; 1234409.C683_0600; -.
DR   PATRIC; fig|1234409.3.peg.550; -.
DR   eggNOG; COG0686; Bacteria.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000016057; Unassembled WGS sequence.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR   CDD; cd05305; L-AlaDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008141; Ala_DH.
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; ALANINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE 1; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRNR:PIRNR000183, ECO:0000256|PIRSR:PIRSR000183-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016057}.
FT   DOMAIN          4..134
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          146..296
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   ACT_SITE        94
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   ACT_SITE        268
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         131
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         218
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         265..268
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         297..300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
SQ   SEQUENCE   365 AA;  38939 MW;  26259B2D64EF2CDD CRC64;
     MKIGVIKDPK QGEGRVGMTP ENVKILTAEG HEVLVDRDAG IGAGFSNEEY QAAGAKIVDT
     EEAWTAPLIV KVKEPMPSEY GYFKEGQIIW GFLHLAANKE CTEEMMKKNM YAVSAENLIV
     DGVQTLLKPM SALAGRRAAY LGANYLEAQY GGEGLLLPGI PGIEAGTAVI LGGGNAAVNA
     CDMLIGMGCH VIILEKSEKQ IAYLEDRYTN DSVEIIPSTQ ESLAENIKKA DVFISTLLIP
     GAKPPKLVTT EMVQSMKKGS VIIDIAIDQG GTVATIEAPT SHADPIFVKY GVVHYAVPNM
     PGAVPRTATI ALSKGNIEYL VDIANKGIEE AVKTNEPIHT AMSVYDGKVV SKALADSIGT
     EYTEL
//
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