ID A5FF25_FLAJ1 Unreviewed; 505 AA.
AC A5FF25;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABQ06188.1};
GN OrderedLocusNames=Fjoh_3171 {ECO:0000313|EMBL:ABQ06188.1};
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ06188.1, ECO:0000313|Proteomes:UP000006694};
RN [1] {ECO:0000313|EMBL:ABQ06188.1, ECO:0000313|Proteomes:UP000006694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC UW101 {ECO:0000313|Proteomes:UP000006694};
RX PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP000685; ABQ06188.1; -; Genomic_DNA.
DR RefSeq; WP_012025157.1; NZ_MUGZ01000015.1.
DR AlphaFoldDB; A5FF25; -.
DR STRING; 376686.Fjoh_3171; -.
DR KEGG; fjo:Fjoh_3171; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_10; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000006694; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino 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; IPR010977; Aromatic_deC.
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; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
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 325
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 505 AA; 57044 MW; 9BBE5E9A2025A90B CRC64;
MQNLLDNAPD VFVKSAADDF YQDIFHENSG TEYANAIELV QKRVAGFLEN TKIPFSGIKP
DEIRNKVEAV NLDQPVQDYE TLWDEIDEIY VNHATAYHLP EYIAHLNCPV VIPALAADVL
ISAINSSQDT YDQSAGGTFI ERKLIAWTGE QIGYNVDCDG IFTGGGSQSN LMGLLLARDY
FALKYLNWNI KLNGCPPDSS KFRIFVSEKS HFSNQKNASI LGLGEQSIVQ VVTDSRYRMD
AEKLKQAILE EKEKGNIPIA IVATAGTTDF GNIDPLSEIS VLAKEHELWM HVDAAYGCGL
LLTDTYKHLL NGIEQADSVT IDYHKSFFQP ICSSAFMVRN KQHLHIIKHH ADYLNPKEQD
YDELPAQINK SLVQSTRRFD ALKLWCTLRY MGRTKLGQYT DTIIETTKQT AEILENDKDF
ELLTDSDLSV LVFRYKLDGW PGDTCKMNLH IKKKMFFNGE VLVASTKVNG IFYLKFTILN
PLTTIAHINN ILSIIKKHGN DYIFS
//
