ID   A0A385C5P9_9GAMM        Unreviewed;       510 AA.
AC   A0A385C5P9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:AXQ22884.1};
GN   ORFNames=BEN71_12735 {ECO:0000313|EMBL:AXQ22884.1};
OS   Acinetobacter wuhouensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1879050 {ECO:0000313|EMBL:AXQ22884.1, ECO:0000313|Proteomes:UP000257257};
RN   [1] {ECO:0000313|EMBL:AXQ22884.1, ECO:0000313|Proteomes:UP000257257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHA60 {ECO:0000313|EMBL:AXQ22884.1,
RC   ECO:0000313|Proteomes:UP000257257};
RX   PubMed=30117799; DOI=10.1099/ijsem.0.002963;
RA   Hu Y., Feng Y., Qin J., Radolfova-Krizova L., Maixnerova M., Zhang X.,
RA   Nemec A., Zong Z.;
RT   "Acinetobacter wuhouensis sp. nov., isolated from hospital sewage.";
RL   Int. J. Syst. Evol. Microbiol. 68:3212-3216(2018).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP031716; AXQ22884.1; -; Genomic_DNA.
DR   RefSeq; WP_068975337.1; NZ_CP031716.1.
DR   AlphaFoldDB; A0A385C5P9; -.
DR   STRING; 1879050.GCA_001696605_03191; -.
DR   KEGG; awu:BEN71_12735; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000257257; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AXQ22884.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}; Transferase {ECO:0000313|EMBL:AXQ22884.1}.
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   510 AA;  56126 MW;  9235587B511A3ECA CRC64;
     MVDFAEHRKA LLCNDAGSIA DYESAMGEAT KAVAAWLQND KMYTGGSIKE LRQAISFNPS
     KEGLGLHQSL ERMVELFLNK SLKVHHPHSL AHLHCPTMVT SQIAEVLINA TNQSMDSWDQ
     SPAGSLMEVQ LIDWLRQKVG YGAGQAGVFT SGGTQSNLMG VLLARDWCIA KNWKDENGNP
     WSVQRDGVPN EAMRNVKVIC SENAHFSVQK NMAMMGMGFQ SVVTVPVNEN AQMDVDALEK
     TMAHLQAEGK IVACVVATAG TTDAGAIDPL KKIREITTKY GAWMHIDAAW GGALILSNDY
     RSMLDGIELS DSITLDFHKH YFQSISCGAF LLKDEANYRF MHYEAEYLNS AYDEEHGVPN
     LVSKSLQTTR RFDALKLWMT IENLGEELYG SMIDHGVKLT REVADYINAT DGLEMLVDPQ
     FASVLFRVIP QGYPVELLDT LNQNVADELF ARGEANIGVT KVGNVQSLKM TTLSPVATLE
     NVQNLLALVL AEADRIKDAI ADGTYTPAID
//