ID DDC_ACIBA Reviewed; 510 AA. AC Q43908; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 26-MAY-2009, entry version 48. DE RecName: Full=L-2,4-diaminobutyrate decarboxylase; DE Short=DABA decarboxylase; DE Short=DABA-DC; DE EC=4.1.1.86; GN Name=ddc; OS Acinetobacter baumannii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=470; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 19606 / NCTC 12156 / CIP 70.34; RX MEDLINE=96337867; PubMed=8772175; DOI=10.1007/s002030050366; RA Ikai H., Yamamoto S.; RT "Sequence analysis of the gene encoding a novel L-2,4-diaminobutyrate RT decarboxylase of Acinetobacter baumannii: similarity to the group II RT amino acid decarboxylases."; RL Arch. Microbiol. 166:128-131(1996). CC -!- CATALYTIC ACTIVITY: L-2,4-diaminobutanoate = propane-1,3-diamine + CC CO(2). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: Amine and polyamine biosynthesis; 1,3-diaminopropane CC biosynthesis; 1,3-diaminopropane from L-aspartate 4-semialdehyde: CC step 2/2. CC -!- SIMILARITY: Belongs to the group II decarboxylase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D55724; BAA09538.1; -; Genomic_DNA. DR BRENDA; 4.1.1.86; 191726. DR GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR InterPro; IPR002129; PyrdxlP-dep_de-COase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1. DR PANTHER; PTHR11999; Pyridoxal_deC; 1. DR Pfam; PF00282; Pyridoxal_deC; 1. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. PE 1: Evidence at protein level; KW Decarboxylase; Direct protein sequencing; Lyase; Pyridoxal phosphate. FT CHAIN 1 510 L-2,4-diaminobutyrate decarboxylase. FT /FTId=PRO_0000147003. FT MOD_RES 319 319 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 510 AA; 56244 MW; 900DF52FD1941B70 CRC64; MVDFAEHRKA LLCNDAQSIA DYESAMGEAV KAVSAWLQNE KMYTGGSIKE LRSAISFQPS KEGMGVQQSL QRMIELFLNK SLKVHHPHSL AHLHCPTMVM SQIAEVLINA TNQSMDSWDQ SPAGSLMEVQ LIDWLRQKVG YGSGQAGVFT SGGTQSNLMG VLLARDWCIA KNWKDENGNP WSVQRDGIPA EAMKNVKVIC SENAHFSVQK NMAMMGMGFQ SVVTVPVNEN AQMDVDALEK TMAHLQAEGK VVACVVATAG TTDAGAIHPL KKIREITNKY GSWMHIDAAW GGALILSNTY RAMLDGIELS DSITLDFHKH YFQSISCGAF LLKDEANYRF MHYEAEYLNS AYDEEHGVPN LVSKSLQTTR RFDALKLWMT IESLGEELYG SMIDHGVKLT REVADYIKAT EGLELLVEPQ FASVLFRVVP EGYPVEFIDS LNQNVADELF ARGEANIGVT KVGNVQSLKM TTLSPVVTVD NVKNLLAQVL AEAERIKDAI ASGNYVPPID //