ID F8KPC3_HELBC Unreviewed; 382 AA.
AC F8KPC3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN OrderedLocusNames=HBZC1_16550 {ECO:0000313|EMBL:CCB80641.1};
OS Helicobacter bizzozeronii (strain CIII-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB80641.1, ECO:0000313|Proteomes:UP000008387};
RN [1] {ECO:0000313|EMBL:CCB80641.1, ECO:0000313|Proteomes:UP000008387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIII-1 {ECO:0000313|EMBL:CCB80641.1,
RC ECO:0000313|Proteomes:UP000008387};
RX PubMed=21705603; DOI=10.1128/JB.05439-11;
RA Schott T., Rossi M., Hanninen M.L.;
RT "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT from human gastric mucosa.";
RL J. Bacteriol. 193:4565-4566(2011).
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; FR871757; CCB80641.1; -; Genomic_DNA.
DR AlphaFoldDB; F8KPC3; -.
DR STRING; 1002804.HBZC1_16550; -.
DR KEGG; hbi:HBZC1_16550; -.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_7; -.
DR Proteomes; UP000008387; 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 PRINTS; PR00368; FADPNR.
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:CCB80641.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008387}.
FT DOMAIN 5..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 152..302
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 382 AA; 41315 MW; 235C4CFC6F77AEEE CRC64;
MIAIGLPKES MDAEFRVALV PEDVAMLVQN ANCQIFVEEN AGLNSGYTNQ QYQQAGAQIV
PTKQAWDQPM ILKCKEPLEH EYALLKEGAT LFSYLDLAYN ASLARMLVDK KILSICTETI
PGPKGNYPIL APMSVVAGNL AAHFIQHYLL ALEHLPGVFG RGVLLRGLAG EPQAKVVVVG
GGVVGLEAAR TLSVMGARVV ILELDFAKLQ DHPYTHLYHL EVLGVNEANI VYALEGALGL
VGAVLQTATA TPKVILRRHL KCMQKGGVVV DVACDLGGCI ETTRQTSTSA PIYLEEDLFH
YGVPNMPGIV AKTSSIAYSH ASLPYVLYFL QHGLKGFLQA KDKVVTQTLG GLSAYQGYLT
QEGIARAFNL PYKDPQEVLA QL
//
