ID A0A099PBP0_9GAMM Unreviewed; 414 AA.
AC A0A099PBP0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:KGK42310.1};
GN ORFNames=LH51_08125 {ECO:0000313|EMBL:KGK42310.1};
OS Nitrincola sp. A-D6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK42310.1, ECO:0000313|Proteomes:UP000029924};
RN [1] {ECO:0000313|EMBL:KGK42310.1, ECO:0000313|Proteomes:UP000029924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-D6 {ECO:0000313|EMBL:KGK42310.1,
RC ECO:0000313|Proteomes:UP000029924};
RA Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA Fernandez S., Ferrer A., Chavez R., Levican G.;
RT "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00009410}.
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:KGK42310.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRLB01000041; KGK42310.1; -; Genomic_DNA.
DR RefSeq; WP_036521324.1; NZ_JRLB01000041.1.
DR AlphaFoldDB; A0A099PBP0; -.
DR STRING; 1545442.LH51_08125; -.
DR OrthoDB; 9805337at2; -.
DR Proteomes; UP000029924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..396
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 414 AA; 45959 MW; 814CE45693D45FBF CRC64;
MSRETIVLGA GIVGVSIAWH LVQRGRKVLL IDRRPPGLET SFGNAGIIQR EAVRPYAFPH
DLKTLLRVLP NRSIDIRYKP SGMFAAASPL LSYYLNSFPG RYKKIIPEYA SIIALSTQEH
DPMIKASGAD ALIQKKGWLE IYRTEAELDA RHKEAQEAAQ QGVVSRRIDR ATLDEMQPGL
SADVCGAIHW QNSWMVESPG DLVQAYAKDF EAKGGEFLEA ELNTIVQNSA NNWTVTTSKG
SHDAAEVVVA LGPWSQDYLA PLNYNFPLFV KRGYHMHYKQ PSIKSTLNYW LMDAEKGYLL
EPMKAGIRLT TGAELANLDA PPAYGQLEAA EKVARKLFPI GERADKEPWK GARPCLPDMK
PIIGPAPKHP GLWLAFGHGH QGFTLGPATG RLLGEMMDNE QTAIDMQPFR ADRF
//
