GenomeNet

Database: UniProt
Entry: K4IBN0_PSYTT
LinkDB: K4IBN0_PSYTT
Original site: K4IBN0_PSYTT 
ID   K4IBN0_PSYTT            Unreviewed;       361 AA.
AC   K4IBN0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
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   OrderedLocusNames=P700755_000287 {ECO:0000313|EMBL:AFU67328.1};
OS   Psychroflexus torquis (strain ATCC 700755 / ACAM 623).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Psychroflexus.
OX   NCBI_TaxID=313595 {ECO:0000313|EMBL:AFU67328.1, ECO:0000313|Proteomes:UP000008514};
RN   [1] {ECO:0000313|EMBL:AFU67328.1, ECO:0000313|Proteomes:UP000008514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA   Bowman J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFU67328.1, ECO:0000313|Proteomes:UP000008514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA   Feng S., Powell S.M., Bowman J.P.;
RT   "The complete sequence of Psychroflexus torquis an extreme psychrophile
RT   from sea-ice that is stimulated by light.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003879; AFU67328.1; -; Genomic_DNA.
DR   RefSeq; WP_015022947.1; NC_018721.1.
DR   AlphaFoldDB; K4IBN0; -.
DR   STRING; 313595.P700755_000287; -.
DR   KEGG; ptq:P700755_000287; -.
DR   eggNOG; COG0686; Bacteria.
DR   HOGENOM; CLU_003376_3_0_10; -.
DR   OMA; HPYYHLY; -.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000008514; Chromosome.
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; 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   NCBIfam; TIGR00518; alaDH; 1.
DR   PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF000183; Alanine_dh; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
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.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000183};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000183}.
FT   DOMAIN          4..137
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          149..297
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT   ACT_SITE        270
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         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT   BINDING         134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         239..240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         267..270
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         279
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT   BINDING         298..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
SQ   SEQUENCE   361 AA;  39133 MW;  22565EA70316822D CRC64;
     MKIGVPIEVK NNESRVSITP AGVFELTKRK HHVYVQTQAG LASGFEDLDY IEAGAEILSS
     LDAVYEKAEM IVKVKEPIEK EYALVREGQI IFTYFHFASS QALTLAMIAS KAVCIAYETV
     EDEDGSLPLL TPMSEVAGRM ATQQGAKYLE KPIRGKGILL GGVPGVPPGK VLVLGAGVVG
     IQAAKMAAGL GAHVTIFDIN MKRLRYVNDI MPSHVVTAFS NEYNIRKHIK TADLIIGAVL
     IPGAKAPKLI TRDMLKDMTP GTVMVDVAVD QGGCFETTRP TTHEDPTYII DDVVHYCVTN
     MPGAVPYTST LALTNVTFPY VLDIAQKGWK EACNSDPSLQ KGLSLDHGKV ICKEILKEMV
     V
//
DBGET integrated database retrieval system