| Tag | Content |
|---|
| CPLM ID | CPLM-006057 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Oxygen-independent coproporphyrinogen-III oxidase |
Protein Synonyms/Alias | Coprogen oxidase; Coproporphyrinogenase |
Gene Name | hemN |
Gene Synonyms/Alias | yihJ; b3867; JW3838 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 81 | IVTRQQHKADQYLDA | acetylation | [1] | | 120 | GTPTYLNKAQISRLM | acetylation | [1] | | 227 | ESFAFTLKRVAELNP | acetylation | [1] | | 256 | FAAQRKIKDADLPSP | acetylation | [1] | | 344 | AQNQKELKQYYQQVD | acetylation | [1] | | 412 | KLLAPLAKDGLVDVD | acetylation | [1] | | 421 | GLVDVDEKGIQVTAK | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX. |
Sequence Annotation | REGION 113 114 S-adenosyl-L-methionine 2 binding.
METAL 62 62 Iron-sulfur (4Fe-4S-S-AdoMet).
METAL 66 66 Iron-sulfur (4Fe-4S-S-AdoMet).
METAL 69 69 Iron-sulfur (4Fe-4S-S-AdoMet).
BINDING 56 56 S-adenosyl-L-methionine 1.
BINDING 68 68 S-adenosyl-L-methionine 2; via carbonyl
BINDING 112 112 S-adenosyl-L-methionine 1; via amide
BINDING 145 145 S-adenosyl-L-methionine 1.
BINDING 172 172 S-adenosyl-L-methionine 2.
BINDING 184 184 S-adenosyl-L-methionine 2.
BINDING 209 209 S-adenosyl-L-methionine 2. |
Keyword | 3D-structure; 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 457 AA |
Protein Sequence | MSVQQIDWDL ALIQKYNYSG PRYTSYPTAL EFSEDFGEQA FLQAVARYPE RPLSLYVHIP 60
FCHKLCYFCG CNKIVTRQQH KADQYLDALE QEIVHRAPLF AGRHVSQLHW GGGTPTYLNK 120
AQISRLMKLL RENFQFNADA EISIEVDPRE IELDVLDHLR AEGFNRLSMG VQDFNKEVQR 180
LVNREQDEEF IFALLNHARE IGFTSTNIDL IYGLPKQTPE SFAFTLKRVA ELNPDRLSVF 240
NYAHLPTIFA AQRKIKDADL PSPQQKLDIL QETIAFLTQS GYQFIGMDHF ARPDDELAVA 300
QREGVLHRNF QGYTTQGDTD LLGMGVSAIS MIGDCYAQNQ KELKQYYQQV DEQGNALWRG 360
IALTRDDCIR RDVIKSLICN FRLDYAPIEK QWDLHFADYF AEDLKLLAPL AKDGLVDVDE 420
KGIQVTAKGR LLIRNICMCF DTYLRQKARM QQFSRVI 457 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc. GO:0051989; F:coproporphyrinogen dehydrogenase activity; IDA:EcoCyc. GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0019353; P:protoporphyrinogen IX biosynthetic process from glutamate; IGI:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |