(data stored in ACNUC1104 zone)

SWISSPROT: D7A015_STAND

ID   D7A015_STAND            Unreviewed;       439 AA.
AC   D7A015;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167};
DE            EC=1.3.98.3 {ECO:0000256|PIRNR:PIRNR000167};
GN   OrderedLocusNames=Snov_0092 {ECO:0000313|EMBL:ADH87429.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87429.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87429.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2
CC         5'-deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen
CC         IX; Xref=Rhea:RHEA:15425, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:57307, ChEBI:CHEBI:57309, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:59789; EC=1.3.98.3;
CC         Evidence={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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002026; ADH87429.1; -; Genomic_DNA.
DR   RefSeq; WP_013164934.1; NC_014217.1.
DR   STRING; 639283.Snov_0092; -.
DR   EnsemblBacteria; ADH87429; ADH87429; Snov_0092.
DR   KEGG; sno:Snov_0092; -.
DR   eggNOG; ENOG4105D4P; Bacteria.
DR   eggNOG; COG0635; LUCA.
DR   HOGENOM; HOG000257214; -.
DR   KO; K02495; -.
DR   OMA; AIHRIQP; -.
DR   OrthoDB; 1130951at2; -.
DR   BioCyc; SNOV639283:G1GLM-92-MONOMER; -.
DR   UniPathway; UPA00251; UER00323.
DR   Proteomes; UP000006633; 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; 3.80.30.20; -; 1.
DR   InterPro; IPR004558; Coprogen_oxidase_HemN.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   PANTHER; PTHR13932; PTHR13932; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000167; HemN; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00538; hemN; 1.
PE   3: Inferred from homology;
DR   PRODOM; D7A015.
DR   SWISS-2DPAGE; D7A015.
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-
KW   2}; Complete proteome {ECO:0000313|Proteomes:UP000006633};
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:ADH87429.1};
KW   Porphyrin biosynthesis {ECO:0000256|PIRNR:PIRNR000167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-1}.
FT   DOMAIN       46    263       Elp3. {ECO:0000259|SMART:SM00729}.
FT   REGION      107    108       S-adenosyl-L-methionine 2 binding.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   METAL        56     56       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   METAL        60     60       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   METAL        63     63       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   BINDING      50     50       S-adenosyl-L-methionine 1.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING      62     62       S-adenosyl-L-methionine 2; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000167-
FT                                1}.
FT   BINDING     106    106       S-adenosyl-L-methionine 1; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     139    139       S-adenosyl-L-methionine 1.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     166    166       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     178    178       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     203    203       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
SQ   SEQUENCE   439 AA;  47470 MW;  D8A6AF99205DF127 CRC64;
     MHSSTLLHAE RAVPRYTSYP TAPHFTGDVG PQNHAAWLST LDTGANLSLY LHVPFCPALC
     FYCGCTTKAT RRPEPVAAYV ARLEREIEFV AAHAGGRTVT HIAWGGGTPS LVGGKALRRL
     YDRISEAFDL DRLTEHAFEL DPREVDEEIA DALAAIGVDR VSLGVQDFSA HVQRAIGRVQ
     PFGTVERAVR LLREAGVSSV NLDLMYGLPH QSERDVRRTA RLATLLGPER LALFGYAHVP
     WMRPNQKMID EKDLPGAAER LQQAEAAREV LLANGYAAVG LDHFARPNDP LARAAAAGHL
     HRNFQGYTVD AADALIGLGA SSISRFPQGF TQNAPDAASY MRAVDAGRFA TARGIAFTPE
     DVARGAYIER LMCDLQVDLD TPTFDEAAPR LASLAADGLV TIEGHHVAMT ATGRPFVRLA
     AAALDARLQQ TTARHSAAV
//

If you have problems or comments...

PBIL Back to PBIL home page