ID A0A099U056_9HELI Unreviewed; 371 AA.
AC A0A099U056;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN Name=ald2 {ECO:0000313|EMBL:STQ85957.1};
GN ORFNames=LS73_002115 {ECO:0000313|EMBL:TLE01094.1}, NCTC12714_00747
GN {ECO:0000313|EMBL:STQ85957.1};
OS Helicobacter muridarum.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=216 {ECO:0000313|EMBL:STQ85957.1, ECO:0000313|Proteomes:UP000255139};
RN [1] {ECO:0000313|EMBL:TLE01094.1, ECO:0000313|Proteomes:UP000029922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:TLE01094.1,
RC ECO:0000313|Proteomes:UP000029922};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:STQ85957.1, ECO:0000313|Proteomes:UP000255139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12714 {ECO:0000313|EMBL:STQ85957.1,
RC ECO:0000313|Proteomes:UP000255139};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UGJE01000002; STQ85957.1; -; Genomic_DNA.
DR EMBL; JRPD02000003; TLE01094.1; -; Genomic_DNA.
DR RefSeq; WP_034556707.1; NZ_UGJE01000002.1.
DR AlphaFoldDB; A0A099U056; -.
DR STRING; 216.LS73_00625; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000029922; Unassembled WGS sequence.
DR Proteomes; UP000255139; Unassembled WGS sequence.
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,
KW ECO:0000313|EMBL:STQ85957.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255139}.
FT DOMAIN 4..139
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 151..299
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 371 AA; 39757 MW; 79291945CD364A4E CRC64;
MNICVPKEIM NHEHRVGLVP SDVALLKDSN PSHKIYIEDG LGSSIGYNNN DYEIAGATVL
KNAKEIWECA DLLVKCKEPT EEEFRFLRKD MVLYSFLDLA YSSELARALI DSKVTSICGE
TIAGPMGNYP ILSAMSEVTG KFAAQHAATL LAANYGGRGM LIGGCAGVSP AKAVVVGGGV
VGMNAAKVLV GMGADVWVLD IDVCKVSNHP LVINNQVKLL YSNENSIAEA LKGADILIGA
VLITATSTPK IITREHLRMM NKGGVVLDVS VDLGGCMETS KQTTHDNPTY IEEDLVHYGV
PNIPGVIART SSITYSYESL PYIKVIANQG WKEMLRMPGA IGGLNAYNGS IALKSIAKAF
NMPYIDTTSL L
//
