ID   A0A010YWC3_9ACTN        Unreviewed;       482 AA.
AC   A0A010YWC3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=PLP-dependent enzyme, glutamate decarboxylase {ECO:0000313|EMBL:EXG79448.1};
GN   ORFNames=CryarDRAFT_0483 {ECO:0000313|EMBL:EXG79448.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG79448.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG79448.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG79448.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) 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:EXG79448.1}.
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DR   EMBL; JFBT01000001; EXG79448.1; -; Genomic_DNA.
DR   RefSeq; WP_051569626.1; NZ_KK073874.1.
DR   AlphaFoldDB; A0A010YWC3; -.
DR   PATRIC; fig|927661.3.peg.468; -.
DR   HOGENOM; CLU_011856_0_4_11; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000021053; 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; 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   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:UP000021053}.
FT   MOD_RES         307
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   482 AA;  49323 MW;  BD167F26351B4952 CRC64;
     MASNASDHGG SRDTALAGNV EALAALLAPV LEALAEGARD RGGPAPAGHP ADLDASWRGA
     FTDFGAPGIG AGAALGELVR MFAAGSVDPA DPRCAAHLHC PPLAVAVAAD AAASALNPSL
     DSWDQAPVGT SLEPAVVAEL ADLVGYPSTA DGVVTTGGSE SNLLGLLLAR EHAIPGAVRS
     GVPAGRYRIF GSEATHFSVH RAAGLLGFGE DAVAPVKTGR DHRLDPDALD EALSRADHTP
     IAVVATAGTT DLGAIDPLPE IAEVARKHRV WLHIDAAYGG GALFSPTLAT KLAGLRAADS
     VGLDLHKLGW QPVAAGVFLT SRATNLAALA RRAEYLNPAD DEDAGYTSLL GRSLRTTRRP
     DALKIAVTLR ALGRDGLGAL VDRCAALAAH AAASIGRQPA LELYQPPNLT TVVFRFTASN
     EVNARLRRAL LAAGTAVIGR TEIDGRVWLK LTLLNPDATH ADVDALLAAV VSAGTQELEA
     AR
//