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UniProtKB/Swiss-Prot entry P33770

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

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Entry information
Entry name HEMF_RHOS4
Primary accession number P33770
Secondary accession number Q3J141
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on January 24, 2006 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name Coproporphyrinogen III oxidase, anaerobic 1
Synonyms Coproporphyrinogenase
Coprogen oxidase
EC 1.3.99.22
Gene name
Name: hemN
OrderedLocusNames: RHOS4_19250
ORFNames: RSP_0317
From
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [TaxID: 272943] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Rhodobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1333567 [NCBI, ExPASy, EBI, Israel, Japan]
Coomber S.A., Jones R.M., Jordan P.M., Hunter C.N.;
"A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. I. Molecular cloning, transposon mutagenesis and sequence analysis of the gene.";
Mol. Microbiol. 6:3159-3169(1992).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
Submitted (SEP-2005) 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
S50573; AAB24393.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000143; ABA79493.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S28440; S28440.
RefSeq YP_353394.1; -.
3D structure databases
ModBase P33770.
Enzyme and pathway databases
BioCyc RSPH272943:RSP_0317-MON; -.
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:0030494; Biological process: bacteriochlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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 P33770.
Genome annotation databases
GeneID 3719077; -.
GenomeReviews CP000143_GR; RHOS4_19250.
KEGG rsp:RSP_0317; -.
NMPDR fig|272943.3.peg.1725; -.
Phylogenomic databases
HOGENOM P33770; -.
Genome annotation databases
CMR P33770; RHOS4_19250.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; 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     Coproporphyrinogen III oxidase, anaerobic 1. PRO_0000109948
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   195   197        ETL -> QSV (in Ref. 1; AAB24393). 
CONFLICT   383   383        D -> E (in Ref. 1; AAB24393). 
CONFLICT   400   409        PRIAEAAEKF -> LAHRRSGREV (in Ref. 1; AAB24393). 
Sequence information
Length: 452 AA [This is the length of the unprocessed precursor] Molecular weight: 50054 Da [This is the MW of the unprocessed precursor] CRC64: 36E1430A36C0D6C9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP ISVYVHVPFC 

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

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

       190        200        210        220        230        240 
IGREQPFENT KACVETLRRY GVHSLNTDLV YGLPHQNRES LAATIDKVLS LRPDRVAIFG 

       250        260        270        280        290        300 
YAHVPWMAKR QKLIDETVLP PDIERHELAN LAARLFTEGG FERIGIDHFA LPDDSMAVAA 

       310        320        330        340        350        360 
RSRKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKSIE EGRLPGYRGH 

       370        380        390        400        410        420 
RMTEEDYLHG RAIEMIMCDF FLDLPALRAR FGEPAETMVP RIAEAAEKFT PFVTVDADGS 

       430        440        450 
MSIAKEGRAL ARMIARLFDA YETPEARYSQ AS
P33770 in FASTA format

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