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UniProtKB/Swiss-Prot entry P95651

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HEMN_RHOS5
Primary accession number P95651
Secondary accession number A4WR64
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on October 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 49)
Name and origin of the protein
Protein name Oxygen-independent coproporphyrinogen III oxidase
Synonyms Coproporphyrinogenase
Coprogen oxidase
EC 1.3.99.22
Gene name
Name: hemN
OrderedLocusNames: Rsph17025_0977
From
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [TaxID: 349102] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Rhodobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Shi J., Bartnikas T.B., Shapleigh J.P.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
"Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U80081; AAB38508.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000661; ABP69878.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T10882; T10882.
RefSeq YP_001167183.1; -.
3D structure databases
ModBase P95651.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051989; Molecular function: coproporphyrinogen dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004109; Molecular function: coproporphyrinogen oxidase activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006779; Biological process: porphyrin biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006638; Elp3/MiaB/NifB.
IPR004558; HemN.
IPR010723; HemN_C.
IPR007197; Radical_SAM.
Graphical view of domain structure.
Pfam PF06969; HemN_C; 1.
PF04055; Radical_SAM; 1.
Pfam graphical view of domain structure.
SMART SM00729; Elp3; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00538; hemN; 1.
ProtoNet P95651.
Genome annotation databases
GeneID 5083193; -.
GenomeReviews CP000661_GR; Rsph17025_0977.
KEGG rsq:Rsph17025_0977; -.
CMR P95651; Rsph17025_0977.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   452  452     Oxygen-independent coproporphyrinogen III oxidase. PRO_0000109949
REGION   112   113  2     S-adenosyl-L-methionine 2 binding (By similarity). 
METAL   60    60        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   64    64        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   67    67        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
BINDING   54    54        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   66    66        S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity). 
BINDING   111   111        S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   144   144        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   171   171        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   183   183        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   208   208        S-adenosyl-L-methionine 2 (By similarity). 
CONFLICT   22    22        S -> C (in Ref. 1; AAB38508). 
CONFLICT   70    70        R -> P (in Ref. 1; AAB38508). 
CONFLICT   197   198        LR -> CA (in Ref. 1; AAB38508). 
CONFLICT   302   302        S -> T (in Ref. 1; AAB38508). 
CONFLICT   306   306        R -> G (in Ref. 1; AAB38508). 
CONFLICT   356   356        G -> A (in Ref. 1; AAB38508). 
CONFLICT   402   402        I -> L (in Ref. 1; AAB38508). 
CONFLICT   443   443        T -> S (in Ref. 1; AAB38508). 
Sequence information
Length: 452 AA [This is the length of the unprocessed precursor] Molecular weight: 49947 Da [This is the MW of the unprocessed precursor] CRC64: 814AFC17EE710CDA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP ISVYIHVPFC 

        70         80         90        100        110        120 
ERLCWFCACR TQGTQTLAPV EAYVGTLLQE LELVKKHLPA GVKAGRLHWG GGTPTILSPE 

       130        140        150        160        170        180 
LIHKLAQAIK AVIPFAEDYE FSVEIDPMMV DEPKIRALSE EGMNRASIGI QDFTDIVQSA 

       190        200        210        220        230        240 
IGREQPFENT RACVETLRRY GVHSLNTDLV YGLPHQNRES LAATIDKVLQ LGPDRVAIFG 

       250        260        270        280        290        300 
YAHVPWMAKR QKLIDENVLP NDMERHELAN LAAKMFTEGG FERIGIDHFA RPDDSMAVAA 

       310        320        330        340        350        360 
RSGKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKAIE EGRLPGYRGH 

       370        380        390        400        410        420 
RMTDEDYLHG RAIEMIMCEF RLDLPALRAR FGEAAETMVP RITEAAAKFA PFITVDEAGS 

       430        440        450 
MSIEAEGRAL TRMIARVFDA YETPEARYSQ AS
P95651 in FASTA format

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