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Database: UniProt/TrEMBL
Entry: Q2SN93_HAHCH
LinkDB: Q2SN93_HAHCH
Original site: Q2SN93_HAHCH 
ID   Q2SN93_HAHCH            Unreviewed;       554 AA.
AC   Q2SN93;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   SubName: Full=Glutamate decarboxylase and related PLP-dependent protein {ECO:0000313|EMBL:ABC27881.1};
GN   OrderedLocusNames=HCH_00996 {ECO:0000313|EMBL:ABC27881.1};
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC27881.1, ECO:0000313|Proteomes:UP000000238};
RN   [1] {ECO:0000313|EMBL:ABC27881.1, ECO:0000313|Proteomes:UP000000238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC27881.1,
RC   ECO:0000313|Proteomes:UP000000238};
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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}.
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DR   EMBL; CP000155; ABC27881.1; -; Genomic_DNA.
DR   RefSeq; WP_011394956.1; NC_007645.1.
DR   AlphaFoldDB; Q2SN93; -.
DR   STRING; 349521.HCH_00996; -.
DR   KEGG; hch:HCH_00996; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000000238; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000238}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   554 AA;  61311 MW;  FF53E5CD22F39182 CRC64;
     MSKTKKIAKA SLETMYRVFT IPEAPNSTLG RIDQKISQNL AGFLQDHIVA VEKDLSEMEK
     DFAESRIPED PVFVSEQTQF LLDKLVSQSV HTASPSFIGH MTSALPYFML PLSKIMIALN
     QNLVKTETSK AFTPLERQVI GMMHRLVYDR DDAYYHEWMH NSSVALGSMC SGGTVANITA
     LWVARNLCFP ADSVFKGVRR EGMFKALKHY GYEGAAVLVS KRGHYSLSKS ADLLGLGSDN
     IIAIPTGANN KIDLQALRAT CEKLRDANVR VISLVGIAGT TETGNIDPLE DMAAIAKEFN
     TYFHVDAAWG GPTLFSNNYK HLLKGIELAD SVTMDAHKQL YVPMGAGLVV FKTPSTSNAI
     EHHAQYIIRQ GSRDLGSKTL EGSRPGMAML IQSGLKIIGR TGYEILIDLG IEKAKTFAAM
     IDQADDFELV SEPELNILTY RYHPVWVRQA FEFADEERRQ AINDCLSRIT KGIQKTQRAR
     GKAFVSRTRL NPAAYDGQAC VVFRVVLANP LTTVEILQDI LEEQRAIAAE DILSERMDEL
     RNLCAIPTAK VAAS
//
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