ID Q2S4A9_SALRD Unreviewed; 842 AA.
AC Q2S4A9;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Tyrosine decarboxylase, putative {ECO:0000313|EMBL:ABC45878.1};
GN OrderedLocusNames=SRU_0837 {ECO:0000313|EMBL:ABC45878.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC45878.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC45878.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
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DR EMBL; CP000159; ABC45878.1; -; Genomic_DNA.
DR RefSeq; YP_444972.1; NC_007677.1.
DR AlphaFoldDB; Q2S4A9; -.
DR STRING; 309807.SRU_0837; -.
DR EnsemblBacteria; ABC45878; ABC45878; SRU_0837.
DR KEGG; sru:SRU_0837; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_005446_0_1_10; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000008674}.
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 462
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 842 AA; 92871 MW; 49449806CF773970 CRC64;
MPRPVGLTPA SRQQLPPAMS TPPSSDALHK AAFLGPKGEN ADELERLLLE VLRDHVFWRR
NFHPRDPRLI DERDKRTEAF DDMSARLRDE LSKILAELKR AAPLYSPRQV AHIVSDPSLP
AFVGYFAGLL YNQNNVVAEV SPETVREERA YFKALAEMVG YPTFLPETLP RDAHARRSAY
SWGHLCSGGT VANLETLWIA RNIRLYPLAV RLVAHQTDAL ASFADLEVTT ATGERAALDA
LSTWRLSNLP IDAITDLHLR IKATLQEGPP ARAQAFQEAL PSVRRAGLAS FLLQYNRAFP
DDPARLPKVF ISQATHYCWQ KNMDVVGLGA DALETVPVDD RIRLDTDALR ERLHACIENR
QPVLGVVSIV GTTEEGAIDP LHEIEAVRQE VGDAGLTFWH HCDAAFGGFF ASLLPKTEDG
NFVPPAQLDD DLAGPDGLLP ADDAEALATL PATDSITIDP HKFGYVPYPA GAVLFRDYHV
RDAIAYKAPY LADEDQSGFG GFLGQWTLEG SRPGAVAVSC YLSQAMVPLT PDGHGRFMEN
CIRANQQLFE ALTERFSAAE GELNLRPFHH PETVAFCFVI APAPGVESVA SLNDYTNRIW
QQMTVDGRED INQYAFLLSR TEVDVAGYAH ILEDLLPTDV VQEAAENGAS LTLLRTCLMN
PFQSDWNTDE GAFPDQVADF LYDVALEESV AHTFPPAPRP SADRHPILVV EQTPRAQEGL
ARYLEHDEKV VAHFDVRSCS AATLKDRRDR MGEVRDLVLH VDPSAPSQAL RITRWLVDEA
QIDPEHLLAV TTQHSNGTDV TARLGALGLP ARNVILESDL LTSTRRLVLQ LSARRSATAG
PS
//
