ID   A0A1Y2ZWQ5_9GAMM        Unreviewed;       281 AA.
AC   A0A1Y2ZWQ5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=D-amino acid aminotransferase {ECO:0000313|EMBL:OTE95198.1};
GN   ORFNames=BCS42_08945 {ECO:0000313|EMBL:OTE95198.1};
OS   Crenothrix sp. D3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Crenotrichaceae; Crenothrix.
OX   NCBI_TaxID=1880899 {ECO:0000313|EMBL:OTE95198.1, ECO:0000313|Proteomes:UP000198219};
RN   [1] {ECO:0000313|EMBL:OTE95198.1, ECO:0000313|Proteomes:UP000198219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D3 {ECO:0000313|EMBL:OTE95198.1};
RA   Oswald K., Graf J.S., Littman S., Tienken D., Brand A., Wehrli B.,
RA   Albertsen M., Daims H., Wagner M., Kuypers M.M., Schubert C.J., Milucka J.;
RT   "Crenothrix are major methane consumers in stratified lakes.";
RL   ISME J. 0:0-0(2017).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC       ECO:0000256|RuleBase:RU004106}.
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:OTE95198.1}.
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DR   EMBL; MBQZ01000094; OTE95198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2ZWQ5; -.
DR   STRING; 1880899.BCS42_08945; -.
DR   Proteomes; UP000198219; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd01558; D-AAT_like; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF10; D-ALANINE AMINOTRANSFERASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:OTE95198.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516}; Transferase {ECO:0000313|EMBL:OTE95198.1}.
SQ   SEQUENCE   281 AA;  31011 MW;  4B1F737B83230C18 CRC64;
     MNNKTVYLNG QYVPLDEAKV SVMDRGFLFG DGVYEVIPCY LGQLFHFQAH VDRLTASLAG
     IRMANPYSTE QWLDIFKPLM DVSENQYIYV QITRGVAPKR DHAFPEKTPP TIFAMCNNIL
     PFAGLETGVK AITLDDSRWQ FCNIKAIALL AHLLHRQDAV EKDCAEAILI NRDGFVTEGA
     ASNLFAVIDG VLLTPPKSNQ ILAGITRDVI LELAAKNNIA CREANISLAE LKTASEIWVT
     SSTREIIPVV ELDGVAVADG KVGAVWHAMN SIFQAYKQSL L
//