ID HEM6_PSE14 Reviewed; 304 AA. AC Q48QH6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Coproporphyrinogen-III oxidase, aerobic; DE Short=Coproporphyrinogenase; DE Short=Coprogen oxidase; DE EC=1.3.3.3; GN Name=hemF; OrderedLocusNames=PSPPH_0026; OS Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., RA Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., RA Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., RA Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., RA Mansfield J.W., Collmer A., Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. RT phaseolicola 1448A reveals divergence among pathovars in genes RT involved in virulence and transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + O(2) + 2 H(+) = CC protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O. CC -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; CC protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step CC 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase CC 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; CP000058; AAZ34851.1; -; Genomic_DNA. DR RefSeq; YP_272340.1; -. DR SMR; Q48QH6; 1-301. DR GeneID; 3557413; -. DR GenomeReviews; CP000058_GR; PSPPH_0026. DR KEGG; psp:PSPPH_0026; -. DR NMPDR; fig|264730.3.peg.224; -. DR HOGENOM; Q48QH6; -. DR OMA; Q48QH6; VKAYLLD. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00333; -; 1. DR InterPro; IPR001260; Coprogen_oxidas. DR InterPro; IPR018375; Coproporphyrinogen-3_ox_CS. DR Gene3D; G3DSA:3.40.1500.10; Coprogen_oxidas; 1. DR PANTHER; PTHR10755; Coprogen_oxidas; 1. DR Pfam; PF01218; Coprogen_oxidas; 1. DR PIRSF; PIRSF000166; Coproporphyri_ox; 1. DR PRINTS; PR00073; COPRGNOXDASE. DR PROSITE; PS01021; COPROGEN_OXIDASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Oxidoreductase; Porphyrin biosynthesis. FT CHAIN 1 304 Coproporphyrinogen-III oxidase, aerobic. FT /FTId=PRO_1000019482. SQ SEQUENCE 304 AA; 34528 MW; 0AB30999D5C68125 CRC64; MSTRTEAVKA YLLDLQDRIC TALEQEDGNA HFVEDAWTRP AGGGGRTRVI ENGAVIEKGG VNFSHVFGSN LPPSASAHRP ELAGRGFEAL GVSLVIHPHN PHVPTSHANV RFFIAEKEGE EPVWWFGGGF DLTPYYGVEE DCVHWHRVAE RACAPFGDDV YPRYKAWCDS YFHLKHRDEP RGIGGLFFDD VNQWDFDTSF AFIRAIGDAF INAYLPIVRR RKAAAYTAQQ REFQEFRRGR YVEFNLVYDR GTLFGLQSGG RTESILMSLP PQVRWGYDWK AAPGSEEARL TEYFLTDRDW LADN //