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Database: UniProt
Entry: A0A1G1Q4C5_9BACT
LinkDB: A0A1G1Q4C5_9BACT
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ID   A0A1G1Q4C5_9BACT        Unreviewed;       332 AA.
AC   A0A1G1Q4C5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, 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=A3G88_04995 {ECO:0000313|EMBL:OGX49009.1};
OS   Omnitrophica WOR_2 bacterium RIFCSPLOWO2_12_FULL_63_16.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801871 {ECO:0000313|EMBL:OGX49009.1, ECO:0000313|Proteomes:UP000177516};
RN   [1] {ECO:0000313|EMBL:OGX49009.1, ECO:0000313|Proteomes:UP000177516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGX49009.1}.
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DR   EMBL; MHHE01000020; OGX49009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1Q4C5; -.
DR   STRING; 1801871.A3G88_04995; -.
DR   Proteomes; UP000177516; 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}.
FT   ACT_SITE        72
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         115
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         142..143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         227..229
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         233
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
FT   BINDING         300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00935"
SQ   SEQUENCE   332 AA;  35860 MW;  C564431F27AF4D51 CRC64;
     MTRPRSTLIL TQSEIDRLID MQTAIRVIRE AFIAQARGET SMPPKVYLDL PGYGDFRAMP
     SALRRPAVCG IKWVNVHPQN QRKGLPTVMG TVILNDPATG FPLAVMDGLS VTRLRTGAAA
     AVAIAALARS RMARVGLVGC GAQALSQLEG LLQVRRVDRI AVWGYRRGEA ARFCRSAGRR
     LGVTLIPVGT VNACVKDADV VITLTPSRRP LVRREWIRPG THLNAIGADA PGKQELDPQI
     LREAVLIVDE PVQAMHGGEI NVPLRKGQLT RRAIHATLGE VLLGRAAGRT RADQITVFDS
     TGLAVHDVAL GYAIYRAALR SHAGHPVALF SP
//
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