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UniProtKB/Swiss-Prot entry A6VPZ6


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

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Entry information
Entry name CYSG_ACTSZ
Primary accession number A6VPZ6
Secondary accession numbers None
Integrated into Swiss-Prot on April 29, 2008
Sequence was last modified on August 21, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 13)
Name and origin of the protein
Protein name Siroheme synthase
Synonyms None
Includes Uroporphyrinogen-III C-methyltransferase
     (Urogen III methylase)
     (EC 2.1.1.107)
     (SUMT)
     (Uroporphyrinogen III methylase)
     (UROM)
Precorrin-2 dehydrogenase
     (EC 1.3.1.76)
Sirohydrochlorin ferrochelatase
     (EC 4.99.1.4)
Gene name
Name: cysG
OrderedLocusNames: Asuc_1691
From
Actinobacillus succinogenes (strain ATCC 55618 / 130Z) [TaxID: 339671] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Actinobacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.;
"Complete sequence of Actinobacillus succinogenes 130Z.";
Submitted (JUN-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
CP000746; ABR75043.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001344978.1; -.
3D structure databases
ModBase A6VPZ6.
Ontologies
GO
GO:0004325; Molecular function: ferrochelatase activity (inferred from electronic annotation from HAMAP).
GO:0043115; Molecular function: precorrin-2 dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0004851; Molecular function: uroporphyrin-III C-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0009236; Biological process: cobalamin biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0019354; Biological process: siroheme biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01646; -; 1.
PBIL [Tree]
InterPro IPR000878; 4pyrrol_Mease.
IPR014777; 4pyrrole_Mease_sub1.
IPR014776; 4pyrrole_Mease_sub2.
IPR006366; CobA_cysG_C.
IPR006367; CysG_synth_N.
IPR016040; NAD(P)-bd.
IPR003043; Uropor_MeTrfase_CS.
Graphical view of domain structure.
Gene3D G3DSA:3.40.1010.10; 4pyrrole_Mease_sub1; 1.
G3DSA:3.30.950.10; 4pyrrole_Mease_sub2; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00590; TP_methylase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01469; cobA_cysG_Cterm; 1.
TIGR01470; cysG_Nterm; 1.
PROSITE PS00839; SUMT_1; 1.
PS00840; SUMT_2; 1.
BLOCKS A6VPZ6.
Genome annotation databases
GeneID 5349272; -.
GenomeReviews CP000746_GR; Asuc_1691.
KEGG asu:Asuc_1691; -.
CMR A6VPZ6; Asuc_1691.
Other
ProtoNet A6VPZ6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cobalamin biosynthesis; Complete proteome; Lyase; Methyltransferase; Multifunctional enzyme; NAD; Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   476  476     Siroheme synthase. PRO_0000330485
REGION   216   456  241     Uroporphyrinogen-III C-methyltransferase. 
Sequence information
Length: 476 AA [This is the length of the unprocessed precursor] Molecular weight: 52367 Da [This is the MW of the unprocessed precursor] CRC64: 244ECFDF5D84F0EC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHYFPVFADL NNRPVLVVGG GGVAARKVNL LLKANADVRI VAQKLNAELT ALFELGHILW 

        70         80         90        100        110        120 
IAGEFNSEQI RNVFLVIAAT DDEYLNERVF RVAESQQKLV NVVDDQARCS FIFPSIIDRN 

       130        140        150        160        170        180 
PIQVAVSSGG TAPVLARLLR EKLEALLPQH LGAMADISGK WRHKVKTKLK TVTERRRFWE 

       190        200        210        220        230        240 
SLFNGRFSQL LKNRQTEAAK KELELQLDKD YRGGFVSLVG AGPGDAGLLT LKGLQEIQQA 

       250        260        270        280        290        300 
DVVLYDALVS DEILELVRRD AKLVFVGKRA QGKQVAQENT NALLVKYAQQ GKRVVRLKGG 

       310        320        330        340        350        360 
DPFVFGRGGE ELEVLAERQI PFSVVPGITA AIGATAYAGI PLTHRDYAQS AVFVTGHRKA 

       370        380        390        400        410        420 
NASDIEWQTL ARSNQTLVIY MGTLKAKDIA ERLQQFGRAG STPIAVISQG TQARQKTHIG 

       430        440        450        460        470 
TLTALAEIAE NAPTPALIVV GEVVTLHDKL AWFGEQKFAQ KRPHFTLDSL RIESVA 

A6VPZ6 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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