ID B4SD94_PELPB Unreviewed; 406 AA.
AC B4SD94;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN OrderedLocusNames=Ppha_2150 {ECO:0000313|EMBL:ACF44353.1};
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF44353.1, ECO:0000313|Proteomes:UP000002724};
RN [1] {ECO:0000313|EMBL:ACF44353.1, ECO:0000313|Proteomes:UP000002724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; CP001110; ACF44353.1; -; Genomic_DNA.
DR RefSeq; WP_012508830.1; NC_011060.1.
DR AlphaFoldDB; B4SD94; -.
DR STRING; 324925.Ppha_2150; -.
DR KEGG; pph:Ppha_2150; -.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_10; -.
DR Proteomes; UP000002724; Chromosome.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
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 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 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACF44353.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002724}.
FT DOMAIN 35..169
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 181..329
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 406 AA; 44089 MW; 3BF3E033EF81CF03 CRC64;
MGYSSDIGNV EFELGAKTLE RWLIKPEKTM EIVLGIPRER LQDERRVAIS PPGVQILVEQ
GIKVIVEKSA GNFCNFTDLA YGEAGATIAE SPEELYQQSN VIVKVSPPMT EELPLFMPGQ
MLISALHLGT ITPDLIKALI EKNITALGFE FIETRDGELP IVRTLSEIAG SLAIQTAAKY
LETGYGGSGI LLGGIAGVPP AWVTIIGAGT VGLFAAQDAL GLGAQVTVID KEINRLRRFE
AFFNRHLVTA IANDHYIAEI AKMSDVLIGA LSPRQKIIKP LVSEQVVKSM KPGSVIIDVS
IDQGACFATS RHTSHTNPIY VKHGVTHYCV PNIPSAVAKT ASFALTNTLL PFLLKLTGHE
TVSEILWKSH SLRKGTYIFK GYVTQKILAE LTDIPFREID MLLAAS
//
