DHA_METMP
ID DHA_METMP Reviewed; 373 AA.
AC Q6LX40;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:15466049};
DE EC=1.4.1.1 {ECO:0000305|PubMed:15659675};
GN Name=ald {ECO:0000303|PubMed:15466049}; OrderedLocusNames=MMP1513;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION AS AN ALANINE DEHYDROGENASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=S2 / LL;
RX PubMed=15659675; DOI=10.1128/jb.187.3.972-979.2005;
RA Moore B.C., Leigh J.A.;
RT "Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for
RT alanine dehydrogenase, alanine racemase, and alanine permease.";
RL J. Bacteriol. 187:972-979(2005).
CC -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC L-alanine. This enzyme is a key factor in the assimilation of L-alanine
CC as an energy source through the tricarboxylic acid cycle.
CC {ECO:0000269|PubMed:15659675}.
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:0000305|PubMed:15659675};
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 dimer (By similarity).
CC {ECO:0000250|UniProtKB:P9WQB1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0QVQ8}.
CC -!- DISRUPTION PHENOTYPE: No growth on either stereoisoform of alanine.
CC {ECO:0000269|PubMed:15659675}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; BX950229; CAF31069.1; -; Genomic_DNA.
DR RefSeq; WP_011171457.1; NC_005791.1.
DR AlphaFoldDB; Q6LX40; -.
DR SMR; Q6LX40; -.
DR STRING; 267377.MMP1513; -.
DR PRIDE; Q6LX40; -.
DR EnsemblBacteria; CAF31069; CAF31069; MMP1513.
DR GeneID; 2762318; -.
DR KEGG; mmp:MMP1513; -.
DR PATRIC; fig|267377.15.peg.1550; -.
DR eggNOG; arCOG06678; Archaea.
DR HOGENOM; CLU_003376_3_0_2; -.
DR OMA; YFPMLMT; -.
DR OrthoDB; 29992at2157; -.
DR BioCyc; MMAR267377:MMP_RS07775-MON; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IMP: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; 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; PS00837; ALADH_PNT_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..373
FT /note="Alanine dehydrogenase"
FT /id="PRO_0000415443"
FT ACT_SITE 96
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 270
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 178..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 239..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 267..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 299..302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 39654 MW; 6B0C51C099774302 CRC64;
MLIGVPKEIK NNENRVAITP AGVEAFVLAG HKVYIEKGAG LGSAITDEEY VAAGAEILAT
AKEVFDTAEM IIKVKEPLKS EFELFKEGQI LFTYLHLAPE PQLTKALLDK KITGIAYETV
QLADRSLPLL TPMSEIAGRM SIQLGAQYLE KQEGGKGVLL GGVPGVEPAE VVIVGGGIVG
TNAAKIAVGM GAKVTILDVN TRRLAYLDDI FGNKVTTLMS NSFNIAKAVK KADLLVGCVL
IPGAKAPKLV SEEMVKSMQP GSVIVDVAID QGGSIETIDR ITTHDNPTYE KFGVIHYAVA
NIPGAVARTS TYALTNDTLP YALQIANKGY KQAVIENPAL LKGLNTLNGK VTYEAVAKAH
DLPYTPAEKA LNE
