DHA_MYCS2
ID DHA_MYCS2 Reviewed; 371 AA.
AC A0QVQ8; Q8KY18;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:12193615, ECO:0000303|PubMed:9785446};
DE EC=1.4.1.1 {ECO:0000269|PubMed:12193615, ECO:0000269|PubMed:9785446};
GN Name=ald {ECO:0000303|PubMed:12193615};
GN OrderedLocusNames=MSMEG_2659, MSMEI_2596;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=12193615; DOI=10.1128/jb.184.18.5001-5010.2002;
RA Feng Z., Caceres N.E., Sarath G., Barletta R.G.;
RT "Mycobacterium smegmatis L-alanine dehydrogenase (Ald) is required for
RT proficient utilization of alanine as a sole nitrogen source and sustained
RT anaerobic growth.";
RL J. Bacteriol. 184:5001-5010(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9785446; DOI=10.1111/j.1574-6968.1998.tb13200.x;
RA Hutter B., Dick T.;
RT "Increased alanine dehydrogenase activity during dormancy in Mycobacterium
RT smegmatis.";
RL FEMS Microbiol. Lett. 167:7-11(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9493394; DOI=10.1099/00221287-144-2-577;
RA Raynaud C., Etienne G., Peyron P., Laneelle M.A., Daffe M.;
RT "Extracellular enzyme activities potentially involved in the pathogenicity
RT of Mycobacterium tuberculosis.";
RL Microbiology 144:577-587(1998).
CC -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC L-alanine. Required for proficient utilization of D- or L-alanine as a
CC nitrogen source. May be required for the adaptation from aerobic growth
CC to anaerobic dormancy. It could be involved in the maintenance of the
CC NAD pool during the shift to an anaerobic dormant state in which oxygen
CC as a terminal electron acceptor becomes limiting.
CC {ECO:0000269|PubMed:12193615, ECO:0000269|PubMed:9785446}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate;
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:0000269|PubMed:12193615, ECO:0000269|PubMed:9785446};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 10 and 11 for the oxidative deamination and
CC between 7 and 7.5 for the reductive amination.
CC {ECO:0000269|PubMed:9785446};
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC -!- SUBUNIT: Homohexamer. Trimer of dimers. {ECO:0000250|UniProtKB:P9WQB1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9493394}.
CC -!- INDUCTION: Induced by both D- and L-alanine under aerobic and anaerobic
CC growth conditions, in exponential and stationary phase. In the absence
CC of inducer, high basal levels of activity are observed in cells growing
CC exponentially under anaerobic conditions (at protein level)
CC (PubMed:12193615). Strongly induced immediately after deflection from
CC aerobic growth. {ECO:0000269|PubMed:12193615,
CC ECO:0000269|PubMed:9785446}.
CC -!- DISRUPTION PHENOTYPE: Non-essential, it can be deleted. Disruption
CC suppresses alanine dehydrogenase activity, impairs the utilization of
CC alanine as a sole nitrogen source while cells grows to a 10-fold
CC decreased saturation density under anaerobic conditions.
CC {ECO:0000269|PubMed:12193615}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; AF304867; AAM44187.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK70995.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39064.1; -; Genomic_DNA.
DR RefSeq; WP_003894041.1; NZ_SIJM01000064.1.
DR RefSeq; YP_886996.1; NC_008596.1.
DR AlphaFoldDB; A0QVQ8; -.
DR SMR; A0QVQ8; -.
DR STRING; 246196.MSMEI_2596; -.
DR EnsemblBacteria; ABK70995; ABK70995; MSMEG_2659.
DR EnsemblBacteria; AFP39064; AFP39064; MSMEI_2596.
DR GeneID; 66734068; -.
DR KEGG; msg:MSMEI_2596; -.
DR KEGG; msm:MSMEG_2659; -.
DR PATRIC; fig|246196.56.peg.2659; -.
DR eggNOG; COG0686; Bacteria.
DR OMA; HPYYHLY; -.
DR OrthoDB; 673280at2; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006524; P:alanine catabolic process; ISS:UniProtKB.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05305; L-AlaDH; 1.
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 PANTHER; PTHR42795; PTHR42795; 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00518; alaDH; 1.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..371
FT /note="Alanine dehydrogenase"
FT /id="PRO_0000419669"
FT ACT_SITE 96
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT ACT_SITE 270
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 178..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 239..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 267..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 298..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
SQ SEQUENCE 371 AA; 38955 MW; A8010101B8EABDCF CRC64;
MLVGIPTEIK NNEYRVAITP AGVAELTRRG HEVIIQAGAG EGSAISDRDF KAAGAEIVNT
ADQVWSEAEL LLKVKEPIEP EYSRMRKGQT LFTYLHLAAS KPCTDALLAS GTTSIAYETV
QTAEGALPLL APMSEVAGRL SAQVGAYHLM RSYGGRGVLM GGVPGVAPAE VVVIGAGTAG
YNAARVAAGM GAHVTVFDLN INTLRRVDGE FGGRIETRYS SSLELEEAVK KADLVIGAVL
VPGAKAPKLV TNSTVAHMKP GAVLVDIAID QGGCFEDSRP TTHDEPTFKV HDTIFYCVAN
MPGAVPRTST FALTNSTMPY VLKLADKGWQ AACASDSALA KGLSTHDGKL LSEAVAKDLD
LPFTDAAQFL A
