ID A6R271_AJECN Unreviewed; 387 AA.
AC A6R271;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HCAG_03729 {ECO:0000313|EMBL:EDN07198.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN07198.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CH476657; EDN07198.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R271; -.
DR STRING; 339724.A6R271; -.
DR VEuPathDB; FungiDB:HCAG_03729; -.
DR HOGENOM; CLU_011856_6_0_1; -.
DR OMA; RRDKEFP; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon 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 PANTHER; PTHR11999:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 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:UP000009297}.
FT MOD_RES 332
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 387 AA; 41792 MW; 836A48A97158538C CRC64;
MSIHPLQSRR DKEFPLQICQ TALSPWTLPV LPTPATISKA RRSLINTLPT TGLGFSETKR
HIVDDIIPGF NGSSLSANYY AFVTGGVTPA ALLADTIVSA YDQNVHVHLP DHSVATDVEH
RALTLLLDLF DLDHKVWVHK TLTTGATGSN VLGLALGREF VLRAAVERKV GADRAVIKSV
GEHGMAEVLL AAGLKGLQVL STYPHSSIGK AAGVLGIGRA NVKSICASGG SENQRPLRFD
FEILEKELSR SDVASIVAVS CGEVNTGHFA TGGLEEFRKI RQLCDKYSAW LHVDGAFGMF
GRILKSGKEF DRVLKGCQGL ELADSITGDA HKLLNVPYDC GIFFSRHADI AEDVCRNPNA
VYLSVGADRL LAGYLSIQLT KFFLTTQ
//
