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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR615 IGR616 IGR614 hctA, - CT743 hemG, - CT745 hemN, - CT746 mfd, - CT748 CT744 hctA, - CT743 hemG, - CT745 hemN, - CT746 mfd, - CT748 CT744 hctA, - CT743 hemG, - CT745 hemN, - CT746 mfd, - CT748 hemE, - CT747 alaS, - CT749 hemE, - CT747 alaS, - CT749 CT744
* Calculated from Protein Sequence

Gene ID: CT746

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
hemN  

Definition:
oxygen-independent coproporphryninogen III oxidase

Gene Start:
868757

Gene Stop:
867387

Gene Length:
1371

Molecular Weight*:
52935

pI*:
7.39

Net Charge*:
2.36

EC:
1.-.-.-  1.3.3.3  

Functional Class:
cofactor biosynthesis; heme and porphyrin  

Pathway: pathway table
Metabolism of Cofactors, Vitamins, and Other Substances; Porphyrin and chlorophyll metabolism

Secondary Evidence:
Lieb C, Siddiqui RA, Hippler B, Jahn D, Friedrich B. 1998. The Alcaligenes eutrophus hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase, is required for heme biosynthesis during anaerobic growth. Arch Microbiol 169(1):52-60. Medline: 9396835.

Homuth,G., Heinemann,M., Zuber,U. and Schumann,W. 1996. The genes of lepA and hemN form a bicistronic operon in Bacillus subtilis.
Microbiology 142(Pt 7): 1641-1649. Medline: 96303504.

Troup B, Hungerer C, Jahn D. 1995. Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase. J Bacteriol 177(11):3326-31. Medline: 7768836.

Xu K, Elliott T. 1994. Cloning, DNA sequence, and complementation analysis of the Salmonella typhimurium hemN gene encoding a putative oxygen-independent coproporphyrinogen III oxidase. J Bacteriol 176(11):3196-203. Medline: 8195073.

Comment:
In E. coli, the coprogen oxidase (HemN) catalyzes the anaerobic transformation of coproporphryninogen-III into protoporphryninogen-IX. This enzyme is the last step in heme biosynthesis in E. coli. See CT745, CT747 and also
CT052.

Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to oxygen-independent coproporphryninogen oxidase sequences, e.g. residues 9-457 are 40% similar to the oxidase from Synechocystis (D90912).

CT746 is orthologous to CPn0889: residues 1-457 are 67% similar to CPn0889. It is also similar to CPn0380, a paralog. CT746 is 28% similar to TP0186, a predicted coproporphyrinogen III
oxidase in T. pallidum. No similarity to M. genitalium.

COGS Summary:  COGS Search
BeTs to 11 clades of COG0635
COG name: Coproporphyrinogen III oxidase and related FeS oxidoreductases
Functional Class:  H
The phylogenetic pattern of COG0635 is -----QvCEBrhUJ--olINx
Number of proteins in this genome belonging to this COG is 2


Blocks Summary:  Blocks Search
Residues 102-112 and 239-249 are matched to block PR00383A, concerned with pro-opiomelanocortin signatures, e.g. in BOVACTM.

ProDom Summary:  Protein Domain Search
Residues 251-382 are 42% similar to a coproporphryninogen oxidase domain as observed in HEMN_ECOLI.
Residues 50-125 and 138-245 support this finding. Residues 26-294 and 161-239
also correspond to uncharacterized domains.

Paralogs:  Local Blast Search
CT746 is weakly paralogous to CT052, also thought to be a coprogen oxidase. Residues 48-345 are 24% similar to CT052.

Pfam Summary:  Pfam Search
Residues 52 to 228 (E-value = 1.7e-21) place CT746 in the Radical_SAM family which is described as Radical SAM superfamily (PF04055)
Residues 310 to 430 (E-value = 5.4e-47) place CT746 in the HemN_C family which is described as HemN C-terminal region (PF06969)

PDB Hit:
None.

Gene Protein Sequence:
MFNINFNFLKGLHQPAPRYTSYPTIVDWESSSDYGYTALERLAQEQDPLS
LYFHIPFCQSMCLYCGCTVVLNRKAEIVDHYIETLIQEMRLAFSLLGGKK
PVSRIHFGGGTPSRLSRAQFERLFTHIHRFFDLSNIEELAIEFDPRSLRE
DADKPLFLHNLGFNRVSLGIQDTQWEVQEAVRRRQSYEESLLAYQLFRDL
KFTGINIDLIYGLPKQTQSSFKQTIEHILDMRPDRLALFSFAHVPWAKPH
QKALRTKDLPSMEEKFAIYSQSRHTLIQEGYQAIGLDHFSLPDDPLTIAL
KNKTLIRNFQGYSLPPEEDLLGFGISATSFIRGIYLQNVKDLREYSETIQ
AGKLATVKGKILSQDDKTRKWVIHTLMCSFSLSKLEFEQRFHERFDRYFA
DSYDRLCGMESAGLIRQDSSSLQVTPLGELFVRVIATAFDHYFLKNIVEK
PLFSKSI

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTTAACATCAATTTCAACTTCCTAAAAGGGCTGCATCAACCAGCTCC
TCGCTATACGAGCTACCCCACCATCGTCGACTGGGAATCCTCCTCAGATT
ATGGCTATACGGCCTTGGAGAGGCTTGCTCAGGAGCAAGATCCTCTTTCT
TTATACTTCCACATCCCATTCTGCCAATCTATGTGTCTATATTGCGGATG
TACTGTTGTTTTAAATAGAAAAGCAGAAATCGTAGATCACTACATAGAGA
CGTTAATCCAAGAAATGCGCCTAGCTTTCTCGTTATTAGGAGGGAAGAAA
CCAGTCTCTAGAATTCACTTTGGTGGCGGGACTCCTAGTCGTTTATCGCG
TGCTCAATTTGAACGTTTGTTCACTCATATCCATCGTTTTTTTGATTTAT
CCAATATCGAAGAACTTGCCATAGAGTTCGATCCTCGAAGTCTCAGAGAG
GATGCCGATAAACCTCTATTCCTTCATAACCTAGGTTTTAATCGTGTGAG
TCTGGGTATTCAGGATACCCAATGGGAAGTTCAAGAAGCTGTTCGTAGAC
GCCAATCTTACGAAGAATCGCTCTTAGCTTATCAACTATTCCGAGACTTA
AAATTCACAGGTATTAATATTGACCTCATTTATGGTCTCCCTAAACAAAC
ACAGTCTAGTTTTAAACAAACCATTGAACATATCTTAGATATGCGGCCAG
ACCGCCTAGCCCTTTTCTCCTTCGCTCATGTACCTTGGGCTAAGCCGCAT
CAAAAGGCTTTGCGCACTAAAGATCTCCCTTCCATGGAAGAGAAATTCGC
GATTTATTCCCAATCTCGGCATACCCTGATCCAGGAAGGCTACCAGGCTA
TTGGTCTAGATCATTTTTCTCTTCCGGATGATCCTCTAACTATCGCCCTT
AAGAACAAAACGTTGATTCGTAATTTCCAAGGGTACTCTCTTCCTCCTGA
AGAAGATCTTCTAGGTTTTGGTATATCGGCAACCAGTTTCATTCGGGGGA
TCTATTTACAAAATGTTAAGGATCTTCGTGAATATTCTGAGACTATTCAG
GCTGGCAAACTAGCAACTGTGAAAGGCAAGATTCTTTCTCAGGATGATAA
AACCCGCAAATGGGTGATTCATACCCTAATGTGTTCTTTTTCATTGTCTA
AACTGGAGTTCGAACAACGGTTTCATGAACGCTTTGATCGATACTTTGCA
GATAGCTATGATCGGCTGTGCGGGATGGAGAGTGCAGGATTAATTCGGCA
AGACTCCTCTTCTTTACAAGTAACTCCTCTTGGAGAGCTTTTTGTACGGG
TCATTGCCACAGCCTTTGACCATTATTTTTTGAAGAACATCGTAGAAAAA
CCTCTTTTTTCGAAGTCTATA


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