ID N9AEJ5_9GAMM Unreviewed; 510 AA.
AC N9AEJ5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:ENV59406.1};
GN ORFNames=F950_01953 {ECO:0000313|EMBL:ENV59406.1};
OS Acinetobacter soli NIPH 2899.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217677 {ECO:0000313|EMBL:ENV59406.1, ECO:0000313|Proteomes:UP000018433};
RN [1] {ECO:0000313|EMBL:ENV59406.1, ECO:0000313|Proteomes:UP000018433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2899 {ECO:0000313|EMBL:ENV59406.1,
RC ECO:0000313|Proteomes:UP000018433};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter soli NIPH 2899.";
RL Submitted (FEB-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:ENV59406.1}.
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DR EMBL; APPV01000011; ENV59406.1; -; Genomic_DNA.
DR RefSeq; WP_004946409.1; NZ_KB849643.1.
DR AlphaFoldDB; N9AEJ5; -.
DR GeneID; 67510680; -.
DR PATRIC; fig|1217677.3.peg.1898; -.
DR HOGENOM; CLU_011856_0_4_6; -.
DR Proteomes; UP000018433; Unassembled WGS sequence.
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; 3.90.1150.170; -; 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; 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 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 510 AA; 56067 MW; BBEB1EA02F321A36 CRC64;
MVDFAEHRKA LLCNDAASIA DYQSAMDDAV KAVAAWLQND KMYTGGSIKE LRSAIAFNPS
KDGLGLHQSL ERMVELFLNK SLKVHHPYSL AHLHCPTMVT SQIAEVLINA TNQSMDSWDQ
SPAGSLMEVQ LIDWLRKKVG YGSGQAGVFT SGGTQSNLMG VLLARDWAIA KNFTDENGQP
WSVQRDGIPA EAMRNIKVIC SENAHFSVQK NMAMMGMGFQ SVVTVPVNEL AQMDVDALEK
TMAHLQAEGK IVACVVATAG TTDAGAIDPL KEIRDITTKY GAWMHIDAAW GGALILSNDY
REMLAGIELS DSITLDFHKH YFQSISCGAF LLKDEANYRF MHYEAEYLNS AYDEEHGVPN
LVSKSLQTTR RFDALKLWMT IEALGEELYG SMIDHGVKLT REVADYIKAT DGLELLVEPQ
FASVLFRVVP QGYPVELLDT LNQNVADELF ARGDANIGVT KVGQVQSLKM TTLSPVATLE
NVQNLLSFVL QEADRIKDAI ASGTYVPAID
//
