ID E0SNY7_IGNAA Unreviewed; 328 AA.
AC E0SNY7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Alanine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00935};
DE Short=AlaDH {ECO:0000256|HAMAP-Rule:MF_00935};
DE EC=1.4.1.1 {ECO:0000256|HAMAP-Rule:MF_00935};
GN Name=ala {ECO:0000256|HAMAP-Rule:MF_00935};
GN OrderedLocusNames=Igag_1121 {ECO:0000313|EMBL:ADM27933.1};
OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignisphaera.
OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM27933.1, ECO:0000313|Proteomes:UP000001304};
RN [1] {ECO:0000313|EMBL:ADM27933.1, ECO:0000313|Proteomes:UP000001304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC {ECO:0000313|Proteomes:UP000001304};
RX PubMed=21304693; DOI=10.4056/sigs.1072907;
RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL Stand. Genomic Sci. 3:66-75(2010).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidative deamination of L-
CC alanine to pyruvate, and the reverse reaction, the reductive amination
CC of pyruvate. {ECO:0000256|HAMAP-Rule:MF_00935}.
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:0000256|HAMAP-Rule:MF_00935};
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. Archaeal alanine dehydrogenase subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00935}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00935}.
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DR EMBL; CP002098; ADM27933.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SNY7; -.
DR STRING; 583356.Igag_1121; -.
DR KEGG; iag:Igag_1121; -.
DR HOGENOM; CLU_042088_3_1_2; -.
DR Proteomes; UP000001304; Chromosome.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR HAMAP; MF_00935; AlaDH_arch; 1.
DR InterPro; IPR012742; Ala_DH_archaeglobus.
DR InterPro; IPR028609; AlaDH_arch-typ.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR NCBIfam; TIGR02371; ala_DH_arch; 1.
DR PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ADM27933.1}; NAD {ECO:0000256|HAMAP-Rule:MF_00935};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00935};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00935,
KW ECO:0000313|EMBL:ADM27933.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001304}.
FT ACT_SITE 70
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 114
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 226..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ SEQUENCE 328 AA; 36207 MW; FCBE5B01CE63F22D CRC64;
MVDILVLNSN DVASILSMKD VISLVENAFR EKGLGRVQMP PKVYLFFSRY DGDLRAMPAY
FEGLDIAGVK IVNSHPMNPT RYGLPTVMAV IYLVDPRGGR PLCIMDGTLI TGMRTGGAAG
VATKYLGRRD SRIVGIIGAG FLARFHLEAF TNVISVERVK IYDVIRSKAE DFAKRYSSIY
GIDIEVANDV REAVYGVDVL ATLTPSREPI VRNEWVSEGM HINAMGADAP GKEELDPDIL
RRAKIVVDDM EQAIHSGEIN VPISRGIIRR EDIYGELGEI VAGIKPGRTS DREITIFDST
GLAIQDIIVA WHVYREAEKR GIGRIISL
//
