ID   A0A090K989_9GAMM        Unreviewed;       512 AA.
AC   A0A090K989;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Putative diaminobutyrate--2-oxoglutarate aminotransferase {ECO:0000313|EMBL:CED60388.1};
GN   ORFNames=MVIS_2446 {ECO:0000313|EMBL:CED60388.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED60388.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; LN554852; CED60388.1; -; Genomic_DNA.
DR   RefSeq; WP_075473118.1; NZ_FRDW01000070.1.
DR   AlphaFoldDB; A0A090K989; -.
DR   STRING; 80854.MVIS_2446; -.
DR   GeneID; 61297327; -.
DR   KEGG; mvs:MVIS_2446; -.
DR   PATRIC; fig|80854.5.peg.2604; -.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000032438; Chromosome complete sequence.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1650.10; PLP-dependent transferases; 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; IPR015422; PyrdxlP-dep_Trfase_small.
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:CED60388.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032438};
KW   Transferase {ECO:0000313|EMBL:CED60388.1}.
FT   MOD_RES         327
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   512 AA;  56137 MW;  2336C3CB6F8743EB CRC64;
     MMKNSNQNQN NDWSDVFIHL DPKAQPHYLN AIEHSARELS AMFTAIDAPY SGLEPAQLNE
     QIMAMPIGKA PIAPLAEIIS NNVNLIGKNA IIVQHPHCIA HLHTPPLIPA LAAETIISAL
     NQSMDSWDQA SSATYVEQKM TDWLCELFGY DLVESATHNG ADGVFTSGGT QSNLMGLLLA
     RDRAVEQISG ESVQKDGLPS YAKKLRILCS QTSHFTVQKS ASLMGLGERA VVTVATDEFG
     CLDMNALTAT IADLQSQDLI PFCVVGTAGT TDLGAIDDLQ AIAAISEQHN MWFHVDGAYG
     GALILSSHKD RLAGIELADS ISTDFHKLFF QPISCGALLI RDNHNFKYLL HHADYLNRET
     DELPNLVDKS IATTKRFDAL KLLMSMQALG TDKFGAMYDH LISLTQDVAA LVTATDKFEL
     LAQPQLSTVL FRYNHLSTNS DVSIEHEEEI SMINQRLRLD LLTAGQAVLG ETKINGYTCL
     KLTILNPCLQ LSDFESLFTK IADFAAEQDY IK
//