ID U4KDK4_9VIBR Unreviewed; 568 AA.
AC U4KDK4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative Aspartate aminotransferase superfamily of pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:CCO61141.1};
GN ORFNames=VIBNI_B1388 {ECO:0000313|EMBL:CCO61141.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO61141.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO61141.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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}.
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DR EMBL; FO203527; CCO61141.1; -; Genomic_DNA.
DR RefSeq; WP_022561620.1; NC_022543.1.
DR AlphaFoldDB; U4KDK4; -.
DR STRING; 28173.VIBNI_B1388; -.
DR KEGG; vni:VIBNI_B1388; -.
DR PATRIC; fig|1260221.3.peg.4991; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000016895; Chromosome 2.
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:CCO61141.1};
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:UP000016895};
KW Transferase {ECO:0000313|EMBL:CCO61141.1}.
FT MOD_RES 358
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 568 AA; 64876 MW; EFF4CCBBE2E73B26 CRC64;
MDISLLKNQQ ANQTTSEFDK LYNEVFRDFF SRDENLWPIY KDPGFAALNQ FRAKHLHPHE
RMSAFTNSND LHQALLSQNH MPAKRMKPTG QPEDVLAFAA ALSKDWENPS SVENVITMPS
DPAIYGAMMG TLANPNLVYS EYAGMAEQLE KNVVRQIANV VGYDQNESTG LFTQGGTFCN
LYGYLLGIRK SLPEAIFKGL DSSQDYRILN SQGGHYSNMT NLSLLGVDIT KKTIRIKVTE
SHEIDLVDLE RSMRACFDVN TVVPTIMLTM GTTDTFAIDQ VKPVYDLRER LCEEYGIQVK
PHIHVDAAVG WSMMFFIDYD FAGNPIGINE ATLRGIESVT ARLRELKYAD SFTVDFQKWG
YVPYTSSLVM IKNKQDMEAL KNDPKNFSYF ENDLQEDTHL QSTIECSRGA TGLFGAYSAL
KYMGLEGYQT LIAHSLQNAN YMRHQLMQDS ACKVVVPENQ GPSVTFRLYN RDFVKFADEE
FEIERHSTDN ETIKARMERN TEYHRHIFNN RGKFGLYTNW VEFISRSNYV GRGIYSYIPG
EKAVFMNPAT QRGHIDQFLE RLYYASGK
//
