ID HEMN_MYCTU Reviewed; 375 AA. AC P71756; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 25-NOV-2008, entry version 65. DE RecName: Full=Probable oxygen-independent coproporphyrinogen III oxidase; DE Short=Coproporphyrinogenase; DE Short=Coprogen oxidase; DE EC=1.3.99.22; GN Name=hemN; OrderedLocusNames=Rv2388c, MT2457; ORFNames=MTCY253.33; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). CC -!- FUNCTION: Anaerobic transformation of coproporphyrinogen-III into CC protoporphyrinogen-IX (By similarity). CC -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + 2 S-adenosyl-L- CC methionine = protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2 CC 5'-deoxyadenosine. CC -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with CC 3 cysteines and an exchangeable S-adenosyl-L-methionine (By CC similarity). CC -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; CC protoporphyrinogen-IX from coproporphyrinogen III (AdoMet route): CC step 1/1. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen III CC oxidase 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; BX842579; CAB03737.1; -; Genomic_DNA. DR EMBL; AE000516; AAK46752.1; ALT_INIT; Genomic_DNA. DR PIR; G70681; G70681. DR RefSeq; NP_216904.1; -. DR RefSeq; NP_336938.1; -. DR GeneID; 885300; -. DR GeneID; 925891; -. DR GenomeReviews; AE000516_GR; MT2457. DR GenomeReviews; AL123456_GR; Rv2388c. DR KEGG; mtc:MT2457; -. DR KEGG; mtu:Rv2388c; -. DR TIGR; MT2457; -. DR TubercuList; Rv2388c; -. DR HOGENOM; P71756; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IEA:EC. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin biosynthetic process; IEA:InterPro. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR010723; HemN_C. DR InterPro; IPR004559; HemN_rel. DR InterPro; IPR007197; Radical_SAM. DR Pfam; PF06969; HemN_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00539; hemN_rel; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Porphyrin biosynthesis; KW S-adenosyl-L-methionine. FT CHAIN 1 375 Probable oxygen-independent FT coproporphyrinogen III oxidase. FT /FTId=PRO_0000109944. FT REGION 68 69 S-adenosyl-L-methionine 2 binding (By FT similarity). FT METAL 15 15 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 19 19 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 22 22 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT BINDING 9 9 S-adenosyl-L-methionine 1 (By FT similarity). FT BINDING 21 21 S-adenosyl-L-methionine 2; via carbonyl FT oxygen (By similarity). FT BINDING 67 67 S-adenosyl-L-methionine 1; via amide FT nitrogen and carbonyl oxygen (By FT similarity). FT BINDING 100 100 S-adenosyl-L-methionine 1 (By FT similarity). FT BINDING 127 127 S-adenosyl-L-methionine 2 (By FT similarity). FT BINDING 139 139 S-adenosyl-L-methionine 2 (By FT similarity). FT BINDING 164 164 S-adenosyl-L-methionine 2 (By FT similarity). SQ SEQUENCE 375 AA; 40334 MW; 6E614EF58AA8FCE9 CRC64; MPGQPFGVYL HVPFCLTRCG YCDFNTYTPA QLGGVSPDRW LLALRAELEL AAAKLDAPTV HTVYVGGGTP SLLGGERLAT LLDMVRDHFV LAPDAEVSTE ANPESTWPEF FATIRAAGYT RVSLGMQSVA PRVLATLDRV HSPGRAAAAA TEAIAEGFTH VNLDLIYGTP GESDDDLVRS VDAAVQAGVD HVSAYALVVE HGTALARRVR RGELAAPDDD VLAHRYELVD ARLSAAGFAW YEVSNWCRPG GECRHNLGYW DGGQWWGAGP GAHGYIGVTR WWNVKHPNTY AEILAGATLP VAGFEQLGAD ALHTEDVLLK VRLRQGLPLA RLGAAERERA EAVLADGLLD YHGDRLVLTG RGRLLADAVV RTLLG //