ID PDAD_CHLTE Reviewed; 181 AA. AC Q8KEX0; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 40. DE RecName: Full=Probable pyruvoyl-dependent arginine decarboxylase; DE Short=PvlArgDC; DE EC=4.1.1.19; DE Contains: DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit beta; DE Contains: DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit alpha; GN Name=pdaD; OrderedLocusNames=CT0562; OS Chlorobium tepidum. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=1097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS; RX MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). CC -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2). CC -!- COFACTOR: Pyruvoyl group (By similarity). CC -!- SIMILARITY: Belongs to the pdaD 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; AE006470; AAM71804.1; -; Genomic_DNA. DR RefSeq; NP_661462.1; -. DR GeneID; 1006157; -. DR GenomeReviews; AE006470_GR; CT0562. DR KEGG; cte:CT0562; -. DR NMPDR; fig|194439.1.peg.556; -. DR TIGR; CT0562; -. DR HOGENOM; Q8KEX0; -. DR OMA; Q8KEX0; YKMSGKI. DR BioCyc; CTEP194439:CT_0562-MON; -. DR BRENDA; 4.1.1.19; 189605. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:HAMAP. DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro. DR HAMAP; MF_01404; -; 1. DR InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand. DR InterPro; IPR002724; Pyruvoyl-dep_arg_deCO2ase. DR Gene3D; G3DSA:3.50.20.10; Pyr-dep_his/arg-deCO2ase_sand; 1. DR Pfam; PF01862; PvlArgDC; 1. DR PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1. DR ProDom; PD010449; DUF44; 1. DR TIGRFAMs; TIGR00286; PvlArgDC; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Lyase; Pyruvate. FT CHAIN 1 42 Pyruvoyl-dependent arginine decarboxylase FT subunit beta (By similarity). FT /FTId=PRO_0000023340. FT CHAIN 43 181 Pyruvoyl-dependent arginine decarboxylase FT subunit alpha (By similarity). FT /FTId=PRO_0000023341. FT SITE 42 43 Cleavage (non-hydrolytic) (By FT similarity). FT MOD_RES 43 43 Pyruvic acid (Ser) (By similarity). SQ SEQUENCE 181 AA; 19976 MW; 85D4571EACD44FF6 CRC64; MSFVPTKVFF TKGVGRHKEY LSSFELALRD AKIEKCNLVT VSSIFPPKCE RISVEEGLKH LKPGQITFAV MARNSTNENN RLISASVGVA LPADESQYGY LSEHHPYGET AEQSGEYAED LAATMLATTL GIEFDPNKDW DEREGIYKMS GKIVNSFNIT ESAEGETGMW TTVISCAVLL P //