ID   D2RU46_HALTV            Unreviewed;       527 AA.
AC   D2RU46;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ADB59115.1};
GN   OrderedLocusNames=Htur_0214 {ECO:0000313|EMBL:ADB59115.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB59115.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB59115.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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; CP001860; ADB59115.1; -; Genomic_DNA.
DR   RefSeq; WP_012941443.1; NC_013743.1.
DR   AlphaFoldDB; D2RU46; -.
DR   STRING; 543526.Htur_0214; -.
DR   GeneID; 8740777; -.
DR   KEGG; htu:Htur_0214; -.
DR   eggNOG; arCOG00027; Archaea.
DR   HOGENOM; CLU_011856_0_4_2; -.
DR   OrthoDB; 56891at2157; -.
DR   Proteomes; UP000001903; 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; 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   InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         334
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   527 AA;  56536 MW;  31AA2F5BB09D4022 CRC64;
     MTGQRSAVDR DRPPAADADP TPPPTAATAF LGGPDGNAAY ADAIERARDV LLESFATSAG
     PYAGTDHETL RERIADLQVV PDDGSSIEDT LETVADDVLA DSVRVHDPGC VAHLHCPPTV
     PALAAELLLS GTNQSMDSFD QAPAASVLEE RVVDACCDLF DYPTGADGVF TGGGTESNFL
     GLLLARDWYC ERRFDRDVQT EGLGPEAASD LRLLCSDAAH FTAEQAAHHL GLGEDAVVSV
     PTDDDRRIDL EALDSTFERL EADGRHPFAI VATAGTTDFG SIDPLAALAD RAADRDLWLH
     VDAAYGGACA ISDRLRPKLE GIDRADSIAV DFHKLFYQPI GCGAFLLRDG DRYRHLERNA
     AYLNPERDDA AGVPNLVSKS TRTTRRFDAL KPFVTFNALG RTGVADCVEY VCELADAVAD
     EIRADPALEL CCDPELSAVV FRYRPETDSE SGSLPTAAVD RVNRAIRDEL LADGEVILAR
     TEVDGTAALK LTLLNPKTTL SDLRDVLEAV VDRGEALETD REVIDSA
//