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Database: UniProt/TrEMBL
Entry: V5TNZ3_HALHI
LinkDB: V5TNZ3_HALHI
Original site: V5TNZ3_HALHI 
ID   V5TNZ3_HALHI            Unreviewed;       350 AA.
AC   V5TNZ3;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=L-tyrosine decarboxylase {ECO:0000313|EMBL:AHB66662.1};
GN   ORFNames=HISP_11840 {ECO:0000313|EMBL:AHB66662.1};
OS   Haloarcula hispanica N601.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=1417673 {ECO:0000313|Proteomes:UP000018572};
RN   [1] {ECO:0000313|EMBL:AHB66662.1, ECO:0000313|Proteomes:UP000018572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N601 {ECO:0000313|EMBL:AHB66662.1,
RC   ECO:0000313|Proteomes:UP000018572};
RX   PubMed=24625874;
RA   Ding J.Y., Chiang P.W., Hong M.J., Dyall-Smith M., Tang S.L.;
RT   "Complete Genome Sequence of the Extremely Halophilic Archaeon Haloarcula
RT   hispanica Strain N601.";
RL   Genome Announc. 2:e00178-14(2014).
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; CP006884; AHB66662.1; -; Genomic_DNA.
DR   RefSeq; WP_014041024.1; NC_023013.1.
DR   AlphaFoldDB; V5TNZ3; -.
DR   GeneID; 23804845; -.
DR   KEGG; hhn:HISP_11840; -.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   Proteomes; UP000018572; Chromosome 1.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
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; IPR020931; MfnA.
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; TIGR03812; tyr_de_CO2_Arch; 1.
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   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
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         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   350 AA;  37717 MW;  ED00FCEBE0B74E49 CRC64;
     MLQRAEPQDF ERVLSSMCTV PHPSAREAAE RFLATNPGDP GTYETIADLE REAVDYLGDI
     TGLSDPAGYV ASGGTEANLQ AIRIARNRAD TDDPNIVAPV HAHFSFTKAA DVLGVELRTA
     PATDYRANME AMGELVDEDT VCVVGVAGST EYGYVDPIPA IADLAETVDA LCHVDAAWGG
     FYLSFTDHDW HFGHANIDTM TIDPHKVGQA AVPAGGLLAR DRSLLDQLAV ETPYLESTDQ
     LTLTGTRSGA GVASAVAAME SLWPAGYEQQ YETSMANADW LADQLSARGH DVVGPELPLV
     AADLSMPMTD ELRDRGWRVS KTGAGEMRVV CMPHVTRSML RSFVADLDWY
//
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