(data stored in ACNUC7421 zone)

SWISSPROT: A8FPD0_SHESH

ID   A8FPD0_SHESH            Unreviewed;       446 AA.
AC   A8FPD0;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   05-JUL-2017, entry version 70.
DE   RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167};
DE            EC=1.3.98.3 {ECO:0000256|PIRNR:PIRNR000167};
GN   OrderedLocusNames=Ssed_0090 {ECO:0000313|EMBL:ABV34703.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34703.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34703.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34703.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Coproporphyrinogen III + 2 S-adenosyl-L-
CC       methionine = protoporphyrinogen IX + 2 CO(2) + 2 L-methionine + 2
CC       5'-deoxyadenosine. {ECO:0000256|PIRNR:PIRNR000167}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000167,
CC         ECO:0000256|PIRSR:PIRSR000167-2};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III
CC       (AdoMet route): step 1/1. {ECO:0000256|PIRNR:PIRNR000167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000167}.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III
CC       oxidase family. {ECO:0000256|PIRNR:PIRNR000167}.
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DR   EMBL; CP000821; ABV34703.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8FPD0; -.
DR   STRING; 425104.Ssed_0090; -.
DR   EnsemblBacteria; ABV34703; ABV34703; Ssed_0090.
DR   KEGG; sse:Ssed_0090; -.
DR   eggNOG; ENOG4105D4P; Bacteria.
DR   eggNOG; COG0635; LUCA.
DR   HOGENOM; HOG000257214; -.
DR   KO; K02495; -.
DR   OMA; TLHRNFM; -.
DR   OrthoDB; POG091H019R; -.
DR   BioCyc; SSED425104:GH7Q-93-MONOMER; -.
DR   UniPathway; UPA00251; UER00323.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004558; Coprogen_oxidase_HemN.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR13932; PTHR13932; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000167; HemN; 1.
DR   SFLD; SFLDF00277; oxygen-independent_coproporphy; 1.
DR   SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00538; hemN; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPD0.
DR   SWISS-2DPAGE; A8FPD0.
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-
KW   2}; Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000167};
KW   Iron {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000313|EMBL:ABV34703.1};
KW   Porphyrin biosynthesis {ECO:0000256|PIRNR:PIRNR000167};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-1}.
FT   DOMAIN       41    261       Elp3. {ECO:0000259|SMART:SM00729}.
FT   REGION      102    103       S-adenosyl-L-methionine 2 binding.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   METAL        51     51       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   METAL        55     55       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   METAL        58     58       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   BINDING      45     45       S-adenosyl-L-methionine 1.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING      57     57       S-adenosyl-L-methionine 2; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000167-
FT                                1}.
FT   BINDING     101    101       S-adenosyl-L-methionine 1; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     134    134       S-adenosyl-L-methionine 1.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     161    161       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     173    173       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     198    198       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
SQ   SEQUENCE   446 AA;  51442 MW;  5D71636E4FDF257B CRC64;
     MIEKYNYSGP RYTSYPTALE FDDSFTEEKL LTSIENSKSD KLSLYVHIPF CAKLCYYCGC
     NKVITRHQHK ADQYIEYLAA EIVKRAPLFK NYLVTQIHWG GGTPTFLSPD QILKLSALIK
     SSFNVADEGE YSIEVDPREI ELSMLDTLKE AGFNRISIGV QDFNKKVQIA VNREQDEQFI
     FDLMAKAKEL GFVSTNIDLI YGLPHQTPET FAETMQRVLD LNPDRLSVFN YAHLPARFAA
     QRKIKDEDLA SPQQKLDMLH QTIETLTGAG YQYIGMDHFA KPDDELSILQ NEGRLHRNFQ
     GYTTQEECDL LGLGVSSISQ IGDCYAQNQK DIRPYYESVD KSGHALWKGC SLNRDDEIRR
     VVIKQLICHF ELDMAQIDEK LGINFEEYFV EDLKLLQTFI DDKLVDITDR KITISPTGRL
     LIRNICICFD VYYREKARQQ QFSRVI
//

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