ID W8VRG6_9FLAO Unreviewed; 399 AA.
AC W8VRG6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=NMS_2230 {ECO:0000313|EMBL:BAO56239.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO56239.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO56239.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO56239.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; AP014548; BAO56239.1; -; Genomic_DNA.
DR RefSeq; WP_041496710.1; NZ_AP014548.1.
DR AlphaFoldDB; W8VRG6; -.
DR STRING; 1454201.NMS_2230; -.
DR HOGENOM; CLU_003376_3_0_10; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000031760; 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}.
FT DOMAIN 32..165
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 177..324
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 399 AA; 43395 MW; A71D46F1D2A54292 CRC64;
MSHILSPFTK DQLIPQEERL EIQRNKQELF IGIPKENQQV EKRICLTPDA VAALTAHGHR
ILMEKGAGLG SSFTDNDYLN SGAELTSDTK KVFSCPTVLK VAPPSDEEIA LIKPQTVLIS
ALQLKTRDKS YFEKLAAKKI TALAFEFIQD DDGNHVATTA LSEISGVAAI LIASELLSSG
TNRTGQLFGN ITGVPPVDVV IMGAGTVGEF AARTAIGLGA QVKVFDNSIS NLRRIKDNVS
QTVYTSTLQP KYLSKALRRC DVVIAALSGK NRAPVVVSQT MVENMKPGAV IIDVSIDMGG
CFETSELTTH ENPTFVKFGI THYCVPNLPS RYSKTASISL SNIFTPYILN IADDGGIEHS
IRMDKGLKNG IYMYHGILTN KSVGEWYNLP CSDVNLLIF
//
