ID A0A0P7XBQ5_9GAMM Unreviewed; 565 AA.
AC A0A0P7XBQ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Putative pyridoxal-dependent aspartate 1-decarboxylase PanP {ECO:0000313|EMBL:KPQ04403.1};
GN Name=panP {ECO:0000313|EMBL:KPQ04403.1};
GN ORFNames=HLUCCO02_07970 {ECO:0000313|EMBL:KPQ04403.1};
OS Idiomarinaceae bacterium HL-53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae.
OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ04403.1, ECO:0000313|Proteomes:UP000053932};
RN [1] {ECO:0000313|EMBL:KPQ04403.1, ECO:0000313|Proteomes:UP000053932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ04403.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-2015) 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}.
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:KPQ04403.1}.
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DR EMBL; LIHO01000008; KPQ04403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7XBQ5; -.
DR STRING; 1298881.Ga0003345_1183; -.
DR PATRIC; fig|1298881.4.peg.1275; -.
DR Proteomes; UP000053932; 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: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; IPR022517; Asp_decarboxylase_pyridox.
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 NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 351
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 565 AA; 62672 MW; AA3167D2A6D0947D CRC64;
MLKFAAQNFA GKNLLARKQI ADVNLESLHR IFTIPEAPDS TLGRIERHLS ENLEGFLTDH
IVAKEKPLHE IEQDFADSAI PENPEFVSDH TETLLNKLVA HSVHTASPRF IGHMTSALPY
FLLPLAKLMV GLNQNLVKIE TSKAFTPLER QVLGMLHHLV YGQNERFYKT WMHSAEHSLG
ALCSGGTIAN ITALWVARNT ALPANEEFAG VGAEGIAAGL QHYGYNRLTI LVSERGHYSL
SKAADVLGIG RKNLVPIATD ENNRIDIKKL EATCKTIQET GGKIMAIVGI AGTTETGHID
PLNEIADIAE QVGAHFHVDA AWGGATLLSS EYRRLMHGIE RADSVTIDAH KQMYVPMGAG
MVLFKAPHSA NSIEHHAEYV IRRGSKDLGS HTLEGSRPGM AMLVYSALHV MGRKGFELLI
NTSIEKARYF AELIEQQNDF ELVTRPELCL LTYRFVPTYL KPALARATAE QIEAINPILN
ALTRFIQKSQ RETGRSFVSR TKLTPSQYFR EPTVVFRTVL ANPLTTETML EEILSEQREI
AETAPRLQKE LRDTAIQVGL LSEPN
//
