(data stored in SCRATCH zone)

SWISSPROT: A0KEY4_AERHH

ID   A0KEY4_AERHH            Unreviewed;       457 AA.
AC   A0KEY4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167};
DE            EC=1.3.98.3 {ECO:0000256|PIRNR:PIRNR000167};
GN   Name=hemN {ECO:0000313|EMBL:ABK38410.1};
GN   OrderedLocusNames=AHA_0272 {ECO:0000313|EMBL:ABK38410.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38410.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38410.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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}.
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DR   EMBL; CP000462; ABK38410.1; -; Genomic_DNA.
DR   RefSeq; WP_011704280.1; NC_008570.1.
DR   RefSeq; YP_854800.1; NC_008570.1.
DR   STRING; 380703.AHA_0272; -.
DR   EnsemblBacteria; ABK38410; ABK38410; AHA_0272.
DR   GeneID; 4490203; -.
DR   KEGG; aha:AHA_0272; -.
DR   PATRIC; fig|380703.7.peg.259; -.
DR   eggNOG; ENOG4105D4P; Bacteria.
DR   eggNOG; COG0635; LUCA.
DR   HOGENOM; HOG000257214; -.
DR   KO; K02495; -.
DR   OMA; LMCNLEL; -.
DR   BioCyc; AHYD380703:G1G7B-273-MONOMER; -.
DR   UniPathway; UPA00251; UER00323.
DR   Proteomes; UP000000756; 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; IPR010723; HemN_C.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
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; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00538; hemN; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KEY4.
DR   SWISS-2DPAGE; A0KEY4.
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-
KW   2}; Complete proteome {ECO:0000313|Proteomes:UP000000756};
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   Porphyrin biosynthesis {ECO:0000256|PIRNR:PIRNR000167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-1}.
FT   DOMAIN       52    272       Elp3. {ECO:0000259|SMART:SM00729}.
FT   REGION      113    114       S-adenosyl-L-methionine 2 binding.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   METAL        62     62       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   METAL        66     66       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   METAL        69     69       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR000167-2}.
FT   BINDING      56     56       S-adenosyl-L-methionine 1.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING      68     68       S-adenosyl-L-methionine 2; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000167-
FT                                1}.
FT   BINDING     112    112       S-adenosyl-L-methionine 1; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     145    145       S-adenosyl-L-methionine 1.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     172    172       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     184    184       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
FT   BINDING     209    209       S-adenosyl-L-methionine 2.
FT                                {ECO:0000256|PIRSR:PIRSR000167-1}.
SQ   SEQUENCE   457 AA;  52915 MW;  C1C6F24AB41E6A70 CRC64;
     MQAEQIVWDQ ALIEKYNYSG PRYTSYPTAL EFNEGFGYPD FVQAASQYPA RNLSLYVHIP
     FCHKLCYYCG CNKVITRHRH KADQYLDFLE QEIKAQAPLF KQRLVTQLHW GGGTPTYLDE
     PQTRRLMAML REHFHFAEEG EISIEVDPRE IELSMLDVLR EIGFNRISLG VQDFNKEVQV
     AVNREQDNDF IRAMLERARE LGFRSTNLDL IYGLPHQNRE SFHHTLEEVL KTDPARLSIF
     NYAHLPSRFA AQHKLKEADM PAPQEKLAML QDTIAFLTGR GYQFIGMDHF AKPDDELAVA
     QREGKLHRNF QGYTTQGDCD LLGLGVSSIS MIGDAYSQNQ KELKAYYGQV ETLGHAQWKG
     CSLNQDDLIR REVIKRLICD FRLNFAAVEQ AHGLVFREYF AEDLKLLQTF IDDGLVRMTE
     EGLEVISTGQ LLIRNICMCF DVYLRNKARQ QQFSRVI
//

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