ID A4C7K3_9GAMM Unreviewed; 542 AA.
AC A4C7K3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Putative cysteine sulfinic acid decarboxylase {ECO:0000313|EMBL:EAR29957.1};
GN ORFNames=PTD2_14094 {ECO:0000313|EMBL:EAR29957.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR29957.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR29957.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR29957.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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|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:EAR29957.1}.
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DR EMBL; AAOH01000002; EAR29957.1; -; Genomic_DNA.
DR RefSeq; WP_009837830.1; NZ_AAOH01000002.1.
DR AlphaFoldDB; A4C7K3; -.
DR STRING; 87626.PTD2_14094; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_6; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000006201; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
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; IPR022517; Asp_decarboxylase_pyridox.
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; TIGR03799; NOD_PanD_pyr; 1.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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}.
FT MOD_RES 337
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 542 AA; 59980 MW; 73DDD24FC1CE8AA9 CRC64;
METKRYAVAS EESLMRIFTV PEAPGSTLAR IEREISSNLA GFLNENIAAI EKPLHEIEKD
FQLAQIPEEP TFVSDHAQQI MEQLVAHSVH TAAPSFIGHM TSALPHFVLP LSKLMVGLNQ
NLVKIETSKA FTPLERQVLG MMHHLVYGQN EGFYQKWMHS AKNALGAFCS GGTVANISAL
WIARNRLLKA DGDFNGIASD GLIAAMLHYG YKGLAVLVSE RGHYSLGKAA DVLGIGRKNF
VAIETDENNK VNVAAMRLKA QELAAKGIKV MAIVGVAGTT ETGNIDPLND MADLAQELNC
HFHIDAAWGG ATLLSNNSRY LLAGVERADS ITIDAHKQMY VPMGAGIVLF KDPEASNAIE
HHAEYILRKG SKDLGSHTLE GSRPGMAMLV HACLNVISRK GYEMLIDKSL KKARYFADLI
KADPDFELIS EPELCLLTYR YVPAKIQALL KTADEETRMD IYIALNRFTA SMQKRQRESG
RSFVSRTRLT PVQYQKLPTV VFRVVLANPL TSEDILQSIL AEQKELAQTD PIFKKYLQKY
LD
//
