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UniProtKB/Swiss-Prot entry Q9ZLH0

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

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Entry information
Entry name HEMN_HELPJ
Primary accession number Q9ZLH0
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 54)
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: jhp_0610
From
Helicobacter pylori J99 (Campylobacter pylori J99) [TaxID: 85963] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Helicobacteraceae; Helicobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/16495; PubMed=9923682 [NCBI, ExPASy, EBI, Israel, Japan]
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori.";
Nature 397:176-180(1999).
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
AE001439; AAD06178.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H71911; H71911.
RefSeq NP_223328.1; -.
3D structure databases
ModBase Q9ZLH0.
Enzyme and pathway databases
BioCyc HPYL85963:JHP0610-MON; -.
Ontologies
GO
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: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).
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.
BLOCKS Q9ZLH0.
ProtoNet Q9ZLH0.
Genome annotation databases
GeneID 890302; -.
GenomeReviews AE001439_GR; jhp_0610.
KEGG hpj:jhp0610; -.
NMPDR fig|85963.1.peg.606; -.
Phylogenomic databases
HOGENOM Q9ZLH0; -.
Genome annotation databases
CMR Q9ZLH0; jhp_0610.
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   457  457     Oxygen-independent coproporphyrinogen III oxidase. PRO_0000109943
REGION   114   115  2     S-adenosyl-L-methionine 2 binding (By similarity). 
METAL   62    62        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   66    66        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
METAL   69    69        Iron-sulfur (4Fe-4S-S-AdoMet) (By similarity). 
BINDING   56    56        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   68    68        S-adenosyl-L-methionine 2; via carbonyl oxygen (By similarity). 
BINDING   113   113        S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   147   147        S-adenosyl-L-methionine 1 (By similarity). 
BINDING   174   174        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   186   186        S-adenosyl-L-methionine 2 (By similarity). 
BINDING   211   211        S-adenosyl-L-methionine 2 (By similarity). 
Sequence information
Length: 457 AA [This is the length of the unprocessed precursor] Molecular weight: 53278 Da [This is the MW of the unprocessed precursor] CRC64: 849CE88D15E1008B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQTIDFEKFS QYSKPGPRYT SYPTAVEFKE NFNEESLKTA FFNHDNLKNP MPLSLYTHLP 

        70         80         90        100        110        120 
FCRSACYFCA CSVIYTSLEE KKVRYISYLK KELALLKNAM DTNREVAQFH YGGGTPTFFS 

       130        140        150        160        170        180 
PPQLDEITQS IQEVFPNFSQ DIEMSCEIDP RHFTKEHMQT LFDRGFNRLS FGVQDFDLEV 

       190        200        210        220        230        240 
QKAIHRIQPF EMVQESVKLA RDYGIKSINF DLIYGLPNQT KEGFLKTLEW VLKLDPDRLA 

       250        260        270        280        290        300 
VFNYAHVPWV KKTMRKIDET LLPSPRDKLE ILESLISFLE KANYQMIGMD HFAKSDNELY 

       310        320        330        340        350        360 
LALQKAELRR NFQGYTTKKF TQTIGIGVTS IGEGSDYYTQ NYKDLHYYEK ALDLGHLPVE 

       370        380        390        400        410        420 
RGVALSQEDV LRKEVIMQMM SNLKLDYSKI EEKFSIDFKA HFKKELEKLK PYEEAGLLSF 

       430        440        450 
NSKGFEMTRT GGMLVRNMAM EFDAYLRGGE KHFSKTL
Q9ZLH0 in FASTA format

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