ID A0A0C1FH95_9FLAO Unreviewed; 386 AA.
AC A0A0C1FH95;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Histidine decarboxylase {ECO:0000313|EMBL:KIA91128.1};
DE EC=4.1.1.22 {ECO:0000313|EMBL:KIA91128.1};
GN ORFNames=OA93_23970 {ECO:0000313|EMBL:KIA91128.1};
OS Flavobacterium sp. KMS.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA91128.1, ECO:0000313|Proteomes:UP000031466};
RN [1] {ECO:0000313|EMBL:KIA91128.1, ECO:0000313|Proteomes:UP000031466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:KIA91128.1,
RC ECO:0000313|Proteomes:UP000031466};
RA Smith A.K., Newman J.;
RT "Flavobacterium sp. KMS.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, 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:KIA91128.1}.
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DR EMBL; JSYP01000058; KIA91128.1; -; Genomic_DNA.
DR RefSeq; WP_039116802.1; NZ_JSYP01000058.1.
DR AlphaFoldDB; A0A0C1FH95; -.
DR STRING; 1566023.OA93_23970; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000031466; Unassembled WGS sequence.
DR GO; GO:0004398; F:histidine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF2; SERINE DECARBOXYLASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031466}.
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 386 AA; 44185 MW; 1E67AC0411238AD6 CRC64;
MIPISESLSV QDSQRLFDLN QYIENARDNF LGYPVSKDFD YSEINHFFKY PINNLGDPFE
NCTYKVQTHE LEIEVVGFFA KLFRADPKDY WGYVTNGSSE SNLYGLYLAR ELHPKAIVYY
SESAHYSIRK NIHLLNIPSI AIRSQENGEI DYDDFENTLK LNRNKPAIVL ATFGTTMKEA
KDDVSKIKNI LKKLAIQDNY IHCDAALSGS YGAFMQPRLP FDFMDGAESI SISGHKFIGS
PIPTGIIITK RSNRDRISKG ISYIGSLDTT ISGSRNGHCP LFLWYAIKKL GVEDLKKRYL
HSLEVAEYCE QRLKTIGIAA WRNPNSITVI FPKTNEEIKL KWQLATQGDI SHIICMSNVT
IQQIDLFIYD IENCTENPDE MTEFTW
//
