DHA_HALED
ID DHA_HALED Reviewed; 371 AA.
AC E1V931;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Alanine dehydrogenase {ECO:0000303|PubMed:28081159};
DE EC=1.4.1.1 {ECO:0000269|PubMed:28081159};
GN Name=ald {ECO:0000303|PubMed:28081159};
GN OrderedLocusNames=HELO_3819 {ECO:0000312|EMBL:CBV43703.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=28081159; DOI=10.1371/journal.pone.0168818;
RA Kindzierski V., Raschke S., Knabe N., Siedler F., Scheffer B.,
RA Pflueger-Grau K., Pfeiffer F., Oesterhelt D., Marin-Sanguino A.,
RA Kunte H.J.;
RT "Osmoregulation in the halophilic bacterium Halomonas elongata: a case
RT study for integrative systems biology.";
RL PLoS ONE 12:E0168818-E0168818(2017).
CC -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC L-alanine. {ECO:0000269|PubMed:28081159}.
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:28081159};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WQB1};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P9WQB1};
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC {ECO:0000250|UniProtKB:P9WQB1}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; FN869568; CBV43703.1; -; Genomic_DNA.
DR RefSeq; WP_013333575.1; NC_014532.2.
DR AlphaFoldDB; E1V931; -.
DR SMR; E1V931; -.
DR STRING; 768066.HELO_3819; -.
DR EnsemblBacteria; CBV43703; CBV43703; HELO_3819.
DR KEGG; hel:HELO_3819; -.
DR eggNOG; COG0686; Bacteria.
DR HOGENOM; CLU_003376_3_0_6; -.
DR OMA; HPYYHLY; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 Magnesium; Metal-binding; NAD; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..371
FT /note="Alanine dehydrogenase"
FT /id="PRO_0000439537"
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 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WQB1"
FT BINDING 203
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; 38504 MW; AAF7C0B7C118F11E CRC64;
MKIAVPKEIK NHEYRVALTP SGARELVGRG HDVIVQAAAG EGAGFSDADF EAAGARLEAD
VAKLWDDAEL ILKVKEPQAE EVARLSAGQT LFTYLHLAAE ESLTKGLLDS GATCIAYETI
TAPEGGLPLL APMSTVAGRM AVQAGAHSLE KAQGGAGILL PGVPGVAPAR VTVIGGGVVG
ENAARMALGL GAEVTVLDKS IPRLETLDDR YQGRMKTVFS TADALEEAVR ESDLIIGAVL
VPGAAAPKLI TRDMLSDMKP GSVLVDVAID QGGCFETSKP TTHAEPTYVV DGVVHYCVAN
MPGAVARTST QALTNATLPF VVALADKGWQ KALADDDHFA AGLNVHDGKL TYRAVAEAFG
LEYVEAASLI G
