ID   A0Z2F6_9GAMM            Unreviewed;       577 AA.
AC   A0Z2F6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Decarboxylase, putative {ECO:0000313|EMBL:EAW42130.1};
GN   ORFNames=MGP2080_12033 {ECO:0000313|EMBL:EAW42130.1};
OS   marine gamma proteobacterium HTCC2080.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW42130.1, ECO:0000313|Proteomes:UP000004719};
RN   [1] {ECO:0000313|EMBL:EAW42130.1, ECO:0000313|Proteomes:UP000004719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW42130.1,
RC   ECO:0000313|Proteomes:UP000004719};
RX   PubMed=20472793; DOI=10.1128/jb.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(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|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:EAW42130.1}.
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DR   EMBL; AAVV01000002; EAW42130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0Z2F6; -.
DR   eggNOG; COG0076; Bacteria.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000004719; 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; 3.40.640.10; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004719}.
FT   MOD_RES         374
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   577 AA;  63408 MW;  8DE5089F7E2E23E3 CRC64;
     MTDGSKSTLF IGPKGEQGRI FSSLWDHLFS VTMQRRSQRF ANDSEWHPLA TTAHDSDQAT
     VLSALEELLG LLREEIPTFS PRYLGHMVSD VSIPALLGHM AMLFENANLA SREAAVVGSA
     LETEAINLLA HMVGLDPKPA RGHFTSGGTL ANFEAVWRAR YRLDHWLALG VWLKVNGHSN
     APLFDWAHCG WSVYHEQMKC HDLSEPDLLP YSSVVMGALA MSRFAREHFE EEWPEPVLLV
     PGNKHYSWPK AANIFGLGRE AVWSCDLDEK GRLSPDALKA QIGRAEVDGR PIMMVVSVAG
     TTELGMIDPV DKVADLLDEL CEHRGLHIWH HIDAAYGGYF CSVLKGDASS LSAASEAALR
     AFPRASSLTL DPHKLGFVPY ACGAFLVPDA NAYLVSNIHA PYLEEIADAK FPSWSTTLEG
     SRAATGPSAV WLSAKIMPLD SQGHGWFLNK SLSITHMLYD VISRVSPNIR MLDSSDTNVM
     CFAIAAEGDS LREANRKTDV VIAHFRESSE LSATRTGLTV ENYGQLVTRT VAGWDGVLDS
     DQLTVVRMVV MNPYLDNEAI VQNIKTQLAD SLRSALN
//