ID   B0RCA8_CLASE            Unreviewed;       372 AA.
AC   B0RCA8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 104.
DE   RecName: Full=Alanine dehydrogenase {ECO:0000256|ARBA:ARBA00072341, ECO:0000256|PIRNR:PIRNR000183};
DE            EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183};
GN   Name=ald {ECO:0000313|EMBL:CAQ02996.1};
GN   OrderedLocusNames=CMS2925 {ECO:0000313|EMBL:CAQ02996.1};
OS   Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ02996.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ02996.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / ICMP 2535 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
CC   -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC       L-alanine. {ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine + NAD(+) + H2O = pyruvate + NH4(+) + NADH + H(+);
CC         Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000183};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005206, ECO:0000256|PIRNR:PIRNR000183}.
CC   -!- SUBUNIT: Homohexamer. Trimer of dimers.
CC       {ECO:0000256|ARBA:ARBA00065528}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}.
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DR   EMBL; AM849034; CAQ02996.1; -; Genomic_DNA.
DR   RefSeq; WP_012300146.1; NC_010407.1.
DR   AlphaFoldDB; B0RCA8; -.
DR   STRING; 31964.CMS2925; -.
DR   GeneID; 29471974; -.
DR   KEGG; cms:CMS2925; -.
DR   eggNOG; COG0686; Bacteria.
DR   HOGENOM; CLU_003376_3_0_11; -.
DR   OrthoDB; 9804592at2; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000001318; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0000286; F:L-alanine dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05305; L-AlaDH; 1.
DR   FunFam; 3.40.50.720:FF:000049; Alanine dehydrogenase; 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; IPR008142; AlaDH/PNT_CS1.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00518; alaDH; 1.
DR   PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF000183; Alanine_dh; 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; PS00836; ALADH_PNT_1; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000183};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001318}.
SQ   SEQUENCE   372 AA;  38874 MW;  DF48AB862A2D47F5 CRC64;
     MKVGIPTEIK NNENRVAATP AGVHELVRRG HEVLVQEGAG LGSSITDADY VEAGATIVAT
     ADEVWGQADL LLKVKEPILE EYPRMRAGQT LFTYLHLAAS RPCTDALVAS GTTAIAYETV
     QLPNRQLPLL QPMSEVAGRL STQVGAYHLM RAAGGRGILL GGVPGTPKAR VVVIGGGVAG
     EHAAANALGM GADVTIIDLS IPRLRELEIR FGGQVQTRVS SAYEIAAQLK DADLVIGSVL
     IPGAQAPKLV TDAMVATMKK GSVLVDIAID QGGCFEGSRP TTHDDPTFAV HDSVYYCVAN
     MPGAVPETST RALTNATLPY VIALAEKGWK RALAEDPALA LGLNVHDGHV TEPHVAAALD
     MPLTPVAEVL AA
//