ID A0A233HHV2_9VIBR Unreviewed; 560 AA.
AC A0A233HHV2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OXX61039.1};
GN ORFNames=B9J89_16480 {ECO:0000313|EMBL:OXX61039.1};
OS Vibrio sp. V15_P4S5T153.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1938669 {ECO:0000313|EMBL:OXX61039.1, ECO:0000313|Proteomes:UP000215241};
RN [1] {ECO:0000313|EMBL:OXX61039.1, ECO:0000313|Proteomes:UP000215241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V15_P4S5T153 {ECO:0000313|EMBL:OXX61039.1,
RC ECO:0000313|Proteomes:UP000215241};
RA Vazquez-Rosas-Landa M.;
RT "High clonality and local adaptation shapes Vibrionaceae linages within an
RT endangered oasis.";
RL Submitted (FEB-2017) 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. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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:OXX61039.1}.
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DR EMBL; NDIJ01000018; OXX61039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A233HHV2; -.
DR Proteomes; UP000215241; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
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 Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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 PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OXX61039.1};
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:OXX61039.1}.
FT MOD_RES 353
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 560 AA; 63511 MW; 204CAEEA0B1E22D6 CRC64;
MKTAYYSVWL DEHANQLNPA FEQIFQTVKA HFFARDPNRW PLYRIHEIAR WLEERKIDAP
TVVNTALQQQ LRHSNTIPRH SSHAIHPFND LALYAAKRSK NWDDPRSVEN VISTPCDPAI
HGALLATIAN PNLVYSEYAG DAIELEKLVV RQIAHLAGYD SDQATGVFTQ GGTFCNLYGY
LLGIRKVLPK SALNGLAGED YRIFNSEAGH YSNMTNLSLL GVDVQGKAIR IKVKDNNEMD
LAELDQQLIF CFKNGIAVPS IMLTFGSTDT FATDDIEQVY AIRERRCQEY AISIKPHIHV
DAAVGWSMLF FQEYDFERNP LSLNRATLTG IESLLPRIKS LQLADSFTVD FQKWGYVPYT
SSLVMLKNKH DLAVLKTDPG YYSYFEHAQR EESHLQSTIE CSRSAVGVFS AYSALQHLGI
EGYQTVIGHT LQNANYLRCQ LAALPHCKVA AVENQGPSVT FRLYDPQKVT CAESMFDQEM
NVARQGSMVD SIVENTLYHR HQFLSHKGQH LNTNWVDSIA RTHYDDTGHC LHIPGEKAVL
MNPNTTRKHI EQFCQNIVRR
//
