ID A0A0S8CCH4_9CHLR Unreviewed; 320 AA.
AC A0A0S8CCH4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE RecName: Full=Putative 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 ORFNames=AMJ70_06910 {ECO:0000313|EMBL:KPK21529.1};
OS Dehalococcoidia bacterium SG8_51_3.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703394 {ECO:0000313|EMBL:KPK21529.1, ECO:0000313|Proteomes:UP000051285};
RN [1] {ECO:0000313|EMBL:KPK21529.1, ECO:0000313|Proteomes:UP000051285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_51_3 {ECO:0000313|EMBL:KPK21529.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK21529.1}.
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DR EMBL; LJTX01000133; KPK21529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CCH4; -.
DR PATRIC; fig|1703394.3.peg.800; -.
DR Proteomes; UP000051285; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
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; IPR028609; AlaDH_arch-typ.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
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 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:KPK21529.1}.
FT ACT_SITE 65
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 135..136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 215..217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT BINDING 288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ SEQUENCE 320 AA; 34212 MW; 357761A13FF046C1 CRC64;
MPTLLLDRNA ARNLMRMADV ISVVEEAVRM CGEGRGKMPP KVYLALEHGD FRAMPAALPG
SAGVKWVNVH PQNPSRGLPS IMAVLIYSDP ETGYPLAIMD ATEITAYRTG ATAAIASKYL
ARRDSRTVGI IGAGFQAHTQ ILAHAELFSA LSINVSDVSH AAVDKLTRSL PQFPIRDCSI
QEAVASDIVC TLTPSRSPII RKEWITPGTH INAVGADAPG KQELDPSILK EAVVIVDDLK
QASGSGEINV PIQKGIYSVG EIYGTLAEVV AGKKKARVND KDITVFDSTG IAVEDIAVAR
LLFEKAQNRG SYPSIDLVGM
//
