ID   A5UI88_HAEIG            Unreviewed;       511 AA.
AC   A5UI88;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CGSHiGG_08300 {ECO:0000313|EMBL:ABR00494.1};
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931 {ECO:0000313|EMBL:ABR00494.1, ECO:0000313|Proteomes:UP000001990};
RN   [1] {ECO:0000313|EMBL:ABR00494.1, ECO:0000313|Proteomes:UP000001990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG {ECO:0000313|EMBL:ABR00494.1,
RC   ECO:0000313|Proteomes:UP000001990};
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABR00494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UI88; -.
DR   KEGG; hiq:CGSHiGG_08300; -.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000001990; Chromosome.
DR   GO; GO:0016831; F:carboxy-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   CDD; cd06450; DOPA_deC_like; 1.
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   InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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         320
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   511 AA;  56543 MW;  4EC9EB43B886BE58 CRC64;
     MSNLKQHKQA LFCNDNEAIN DYETAMNNAV QAVSAWLKNE KMYTGGSIKQ MRALISGFNP
     TKEGMGVQKS LDHLVEIFLN PSLKVHHPHS LAHLHCPTMV TSQIAEVLIN ATNQSMDSWD
     QSPAGSIMEE HLINWLRQKA GYGEGTSGVF TSGGTQSNLM GVLLARDWAI ANHWKNEDGS
     EWSVQRDGIP AEAMQKVKVI CSENAHFSVQ KNMAMMGMGF QSVVTVPSNA NAQMDLIALK
     QTLAQLKADG KITACIVATA GTTDAGAIDD LKAIRKLADE YQAWLHVDAA WGGALLLSKD
     YRYFLDGIEL TDSITLDFHK HFFQTISCGA FLLKDPANYR FIDYKADYLN SEYDEAHGVP
     NLVAKSLQTT RRFDALKLWF TLEALGEDLY ASMIDHGVKL TKEVEQYIND TPALEMLVPS
     QFASVLFRVV PKDYPAEFID ALNQNVADEL FARGEANIGV TKVGDKQSLK MTTLSPIATL
     ENVKALLTQV LTEANRIKDD IKNSTYTPPI D
//