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Entry information : HdDiHCcP
Entry ID 5076
Creation 2007-03-27 (Filippo Passardi)
Last sequence changes 2007-03-27 (Filippo Passardi)
Sequence status complete
Reviewer Marcel Zamocky
Last annotation changes 2008-05-16 (Christophe Dunand)
Peroxidase information: HdDiHCcP
Name HdDiHCcP
Class Di-haem cytochrome C peroxidase    [Orthogroup: DiHCcP001]
Taxonomy Bacteria Proteobacteria Gammaproteobacteria Pasteurellaceae Haemophilus
Organism Haemophilus ducreyi    [TaxId: 730 ]
Cellular localisation N/D
Tissue type N/D
Inducer N/D
Repressor N/D
Best BLASTp hits
Perox score E-value HdDiHCcP
start..stop		 S start..stop
AsuDiHCcP 738 0 1..458 1..459
VfDiHCcP 445 1.67e-154 1..461 1..461
ZmomDiHCcP 407 2.87e-139 1..457 3..464
GoDiHCcP 392 3.89e-133 1..457 7..469
Literature and cross-references HdDiHCcP
Literature Zaretzky,F.R., Cole,L.E. and Kawula,T.H. Identification of a putative oxaloacetate decarboxylase and cytochrome-c-peroxidase in Haemophilus ducreyi. Unpublished. Submitted (29-OCT-1999).
Protein ref. GenPept:   AAF14629 UniProtKB:   Q9RF96
DNA ref. GenBank:   AF200362 (3955..5339)
Protein sequence: HdDiHCcP
Sequence Properties
first value : protein
second value (mature protein)
Length (aa):   %s   461
PWM (Da):   %s   51667.74 Transmb domain:   %s   i5-27o
PI (pH):   %s   6.09
Sequence
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*.........1 .........2 .........3 .........4 .........5 .........6 .........7 .........8 .........9 .........0 .........1 .........2
MKKYLLSALA VGGIGYFSLV GYAYWFDTEQ APKLLEKAAL PESHQAVANI MFENGRHYCH TPDAELPAYA KLPIASQLMA QDIERGTRFF RFDRLLDGMK DPSKLSEADL AKLEQVIRND  EMPIAKYVHV HWGSRPDETQ KKPFLDWIHQ QRKAHFLPNV ESANANRLVQ PIPDQLTTDP HKVALGEALY FDDRLSGDGS IQCNTCHLLT QGGVDNLPVS EGIDGKKGGI NAPSVFNAAF  NKWQFWDGRA KTLADQAGGP PTNPVEMGSK TWDEILARLD QDEEFKQRFF AVYPHLTQET VTDAIGEFEK TLITPNSAFD RFLKGDQTAL TDVQKRGYEH FQKAKCDTCH TGTAMGGQSF 
EYLGLYGDYF KDRGTPLTEA DEGRFAVTKD PSDKHRFKVP TLRNVALTAP YMHDASAKDL KEAVRIMGHY QSNKDFSENE LKEIVAFLES LTGEYQGKHP N 

Retrieve as FASTA  
Remarks Genomic. Strain="35000". Unusually long DiHCcP (START codon is 100 a.a. earlier than usual). Note that the long 5' fragment includes a third CxxCH heme-binding motif. High similarity with other DiHCcP, but no "critical" histidine residue after the first CxxCH motif (see Wang Y. et al. (2003), Biochemistry, pp.7318-7325 and Dias J.M. et al. (2004), Structure, pp.961-973): does this protein still have peroxidase activity?