ID B6JP32_HELP2 Unreviewed; 380 AA.
AC B6JP32;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN Name=ald {ECO:0000313|EMBL:ACJ08660.1};
GN OrderedLocusNames=HPP12_1514 {ECO:0000313|EMBL:ACJ08660.1};
OS Helicobacter pylori (strain P12).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508 {ECO:0000313|EMBL:ACJ08660.1, ECO:0000313|Proteomes:UP000008198};
RN [1] {ECO:0000313|Proteomes:UP000008198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12 {ECO:0000313|Proteomes:UP000008198};
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACJ08660.1, ECO:0000313|Proteomes:UP000008198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12 {ECO:0000313|EMBL:ACJ08660.1,
RC ECO:0000313|Proteomes:UP000008198};
RX PubMed=20478826; DOI=10.1093/nar/gkq378;
RA Fischer W., Windhager L., Rohrer S., Zeiller M., Karnholz A., Hoffmann R.,
RA Zimmer R., Haas R.;
RT "Strain-specific genes of Helicobacter pylori: genome evolution driven by a
RT novel type IV secretion system and genomic island transfer.";
RL Nucleic Acids Res. 38:6089-6101(2010).
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; CP001217; ACJ08660.1; -; Genomic_DNA.
DR RefSeq; WP_000152044.1; NC_011498.1.
DR AlphaFoldDB; B6JP32; -.
DR KEGG; hpp:HPP12_1514; -.
DR HOGENOM; CLU_003376_3_0_7; -.
DR Proteomes; UP000008198; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..135
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 152..300
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 380 AA; 40951 MW; FAF1C39309AFFA32 CRC64;
MTIGLVKESM DLESRVALVP DDVALIIQKG VEVLVENNAG ANSGYSNEAY ESVGAKIVDS
KTAWGQDLVV KCKEPLEHEY PLLKEKATLF SYLDLAYQKS LCEMFIDKKI TSICTETIAG
PKNDYPILAP MSVVAGRLAA HLIQHYLLAL EHVKGFMGKG VMLGGLSGAQ RAKIVVVGGG
VVGMESAKVL SQMGAKVTIL ELDYAKLQNH PYYHLYDLEV LSVNEANIIQ ALNGAVGLVG
AVLVTASQTP KVILRRHLKC MQKQGVVIDV ACDLGGCIET IHQTSHSNPV YVEEDLLHYG
VPNMPGIAAK TSSTAYSHAS APYLLYYLEH GLKGFLTANT KIVANTLGGL SAYNGYITQE
GIAKAFNLAF KSPLEVLKEL
//
