ID   A0A2V5L360_9MICC        Unreviewed;       391 AA.
AC   A0A2V5L360;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:PYI65538.1};
GN   ORFNames=CVV68_17605 {ECO:0000313|EMBL:PYI65538.1};
OS   Arthrobacter livingstonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=670078 {ECO:0000313|EMBL:PYI65538.1, ECO:0000313|Proteomes:UP000247832};
RN   [1] {ECO:0000313|EMBL:PYI65538.1, ECO:0000313|Proteomes:UP000247832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LI2 {ECO:0000313|EMBL:PYI65538.1,
RC   ECO:0000313|Proteomes:UP000247832};
RA   Liu Q., Xin Y.-H.;
RT   "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT   and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT   glacialis sp. nov.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PYI65538.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QJVD01000023; PYI65538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5L360; -.
DR   OrthoDB; 5918420at2; -.
DR   Proteomes; UP000247832; Unassembled WGS sequence.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047126; F:N5-(carboxyethyl)ornithine synthase activity; IEA:InterPro.
DR   CDD; cd12181; ceo_syn; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR046951; CEOS.
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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          11..148
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          151..313
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   391 AA;  42440 MW;  71BD28374D13E02B CRC64;
     MMAASTPLRL GVLGTSRKPD ERRAPIHPDH FSNIEQEIRD RMVVEEGYGV QFGVSDAALA
     ALVGAVSPRD EVIAGADIVL LPKPLAADLA DLKDGQILWG WPHCVQDRAL TQLAIDKKLT
     LIAFEAMNHW GSDGGFGLHV FHKNNELAGY SSVMHSLSLI GSTGDYGRRL KAVVIGFGAT
     ARGAVTALRA LGIYDVQVLT RRSVAAVASP IHAVEMVQFE FAPEPPYPGF VMLDDGDAPL
     ATFLAEADIV VNCTLQDPNA PMTYLTEADL AVFRPGSLIV DVSCDEGMGF SWARNTTFVD
     PMFTVGGNIN YYAVDHSPSY LWNSATWEIS EGLLPFIEPV LAGPAAWQEN ETIRRAIEIQ
     DGVIGNPAIL QFQRRQESYP HLPLPEAGFE S
//