HEM6_ECOLI
ID HEM6_ECOLI Reviewed; 299 AA.
AC P36553;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase {ECO:0000255|HAMAP-Rule:MF_00333};
DE Short=CPO {ECO:0000255|HAMAP-Rule:MF_00333};
DE Short=Coprogen oxidase {ECO:0000255|HAMAP-Rule:MF_00333};
DE Short=Coproporphyrinogenase {ECO:0000255|HAMAP-Rule:MF_00333};
DE EC=1.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00333};
GN Name=hemF {ECO:0000255|HAMAP-Rule:MF_00333};
GN OrderedLocusNames=b2436, JW2429;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8300522; DOI=10.1128/jb.176.3.673-680.1994;
RA Troup B., Jahn M., Hungerer C., Jahn D.;
RT "Isolation of the hemF operon containing the gene for the Escherichia coli
RT aerobic coproporphyrinogen III oxidase by in vivo complementation of a
RT yeast HEM13 mutant.";
RL J. Bacteriol. 176:673-680(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, MASS SPECTROMETRY, ACTIVITY REGULATION, SUBUNIT, AND
RP CRYSTALLIZATION.
RX PubMed=13129604; DOI=10.1016/s0378-1097(03)00531-7;
RA Breckau D., Mahlitz E., Sauerwald A., Layer G., Jahn D.;
RT "Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli:
RT one-step purification and biochemical characterisation.";
RL FEMS Microbiol. Lett. 226:31-37(2003).
RN [6]
RP PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, MUTAGENESIS OF HIS-96; HIS-106; HIS-145 AND HIS-175,
RP ACTIVITY REGULATION, MASS SPECTROMETRY, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=12975365; DOI=10.1074/jbc.m308553200;
RA Breckau D., Mahlitz E., Sauerwald A., Layer G., Jahn D.;
RT "Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia
RT coli is stimulated by manganese.";
RL J. Biol. Chem. 278:46625-46631(2003).
CC -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic
CC oxidative decarboxylation of propionate groups of rings A and B of
CC coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-
CC IX. {ECO:0000255|HAMAP-Rule:MF_00333, ECO:0000269|PubMed:12975365,
CC ECO:0000269|PubMed:13129604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O +
CC protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00333,
CC ECO:0000269|PubMed:12975365, ECO:0000269|PubMed:13129604};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00333,
CC ECO:0000269|PubMed:12975365};
CC -!- ACTIVITY REGULATION: Inhibited by protoporphyrinogen-IX, by metal
CC chelator (EGTA) and by low concentrations of heavy metal ions.
CC {ECO:0000269|PubMed:12975365, ECO:0000269|PubMed:13129604}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for coproporphyrinogen-III (at pH 6 at 37 degrees Celsius)
CC {ECO:0000269|PubMed:12975365, ECO:0000269|PubMed:13129604};
CC KM=3.1 uM for coproporphyrinogen-III (at pH 7)
CC {ECO:0000269|PubMed:12975365, ECO:0000269|PubMed:13129604};
CC Vmax=1.3 umol/min/mg enzyme (at pH 6 at 37 degrees Celsius)
CC {ECO:0000269|PubMed:12975365, ECO:0000269|PubMed:13129604};
CC Note=kcat is 0.17 min(-1) for decarboxylation of coproporphyrinogen-
CC III (at pH 6 and at 37 degrees Celsius).
CC {ECO:0000269|PubMed:12975365};
CC pH dependence:
CC Optimum pH is between 6 and 7. {ECO:0000269|PubMed:12975365,
CC ECO:0000269|PubMed:13129604};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00333}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00333,
CC ECO:0000269|PubMed:12975365, ECO:0000269|PubMed:13129604}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MASS SPECTROMETRY: Mass=35390; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:13129604};
CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000255|HAMAP-Rule:MF_00333}.
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DR EMBL; X75413; CAA53167.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75489.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16319.1; -; Genomic_DNA.
DR PIR; B36964; B36964.
DR RefSeq; NP_416931.1; NC_000913.3.
DR RefSeq; WP_000801365.1; NZ_LN832404.1.
DR AlphaFoldDB; P36553; -.
DR SMR; P36553; -.
DR BioGRID; 4260574; 13.
DR IntAct; P36553; 3.
DR STRING; 511145.b2436; -.
DR PaxDb; P36553; -.
DR PRIDE; P36553; -.
DR DNASU; 946908; -.
DR EnsemblBacteria; AAC75489; AAC75489; b2436.
DR EnsemblBacteria; BAA16319; BAA16319; BAA16319.
DR GeneID; 946908; -.
DR KEGG; ecj:JW2429; -.
DR KEGG; eco:b2436; -.
DR PATRIC; fig|1411691.4.peg.4295; -.
DR EchoBASE; EB2106; -.
DR eggNOG; COG0408; Bacteria.
DR HOGENOM; CLU_026169_0_1_6; -.
DR InParanoid; P36553; -.
DR OMA; HDKGTLF; -.
DR PhylomeDB; P36553; -.
DR BioCyc; EcoCyc:COPROGENOXI-MON; -.
DR BioCyc; MetaCyc:COPROGENOXI-MON; -.
DR BRENDA; 1.3.3.3; 2026.
DR UniPathway; UPA00251; UER00322.
DR PRO; PR:P36553; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0046906; F:tetrapyrrole binding; IMP:EcoliWiki.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IBA:GO_Central.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:EcoCyc.
DR Gene3D; 3.40.1500.10; -; 1.
DR HAMAP; MF_00333; Coprogen_oxidas; 1.
DR InterPro; IPR001260; Coprogen_oxidase_aer.
DR InterPro; IPR036406; Coprogen_oxidase_aer_sf.
DR InterPro; IPR018375; Coprogen_oxidase_CS.
DR PANTHER; PTHR10755; PTHR10755; 1.
DR Pfam; PF01218; Coprogen_oxidas; 1.
DR PIRSF; PIRSF000166; Coproporphyri_ox; 1.
DR PRINTS; PR00073; COPRGNOXDASE.
DR SUPFAM; SSF102886; SSF102886; 1.
DR PROSITE; PS01021; COPROGEN_OXIDASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Heme biosynthesis; Manganese;
KW Metal-binding; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..299
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT /id="PRO_0000109894"
FT REGION 240..275
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 108..110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305"
FT BINDING 258..260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT SITE 175
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT MUTAGEN 96
FT /note="H->L: Complete loss of oxidase activity and absence
FT of manganese ions."
FT /evidence="ECO:0000269|PubMed:12975365"
FT MUTAGEN 106
FT /note="H->L: Complete loss of oxidase activity and absence
FT of manganese ions."
FT /evidence="ECO:0000269|PubMed:12975365"
FT MUTAGEN 145
FT /note="H->L: Complete loss of oxidase activity and absence
FT of manganese ions."
FT /evidence="ECO:0000269|PubMed:12975365"
FT MUTAGEN 175
FT /note="H->L: Complete loss of oxidase activity and absence
FT of manganese ions."
FT /evidence="ECO:0000269|PubMed:12975365"
FT MUTAGEN 274
FT /note="W->L: Complete loss of oxidase activity."
SQ SEQUENCE 299 AA; 34323 MW; 53667E5C7B6D0198 CRC64;
MKPDAHQVKQ FLLNLQDTIC QQLTAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV
NFSHVHGEAM PASATAHRPE LAGRSFEAMG VSLVVHPHNP YVPTSHANVR FFIAEKPGAD
PVWWFGGGFD LTPFYGFEED AIHWHRTARD LCLPFGEDVY PRYKKWCDEY FYLKHRNEQR
GIGGLFFDDL NTPDFDRCFA FMQAVGKGYT DAYLPIVERR KAMAYGERER NFQLYRRGRY
VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYQP KDGSPEAALS EFIKVRDWV
