HEM6_SYNY3
ID HEM6_SYNY3 Reviewed; 340 AA.
AC P72848;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
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}; OrderedLocusNames=sll1185;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, COFACTOR, AND
RP INDUCTION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=20194361; DOI=10.1093/pcp/pcq023;
RA Goto T., Aoki R., Minamizaki K., Fujita Y.;
RT "Functional differentiation of two analogous coproporphyrinogen III
RT oxidases for heme and chlorophyll biosynthesis pathways in the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL Plant Cell Physiol. 51:650-663(2010).
CC -!- FUNCTION: Involved in the heme and chlorophyll biosynthesis. Catalyzes
CC the aerobic oxidative decarboxylation of propionate groups of rings A
CC and B of coproporphyrinogen-III to yield the vinyl groups in
CC protoporphyrinogen-IX. {ECO:0000255|HAMAP-Rule:MF_00333,
CC ECO:0000269|PubMed:20194361}.
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:20194361};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000305|PubMed:20194361};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00333}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:20194361}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow under
CC aerobic conditions, with accumulation of coproporphyrin-III.
CC {ECO:0000269|PubMed:20194361}.
CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000255|HAMAP-Rule:MF_00333}.
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DR EMBL; BA000022; BAA16863.1; -; Genomic_DNA.
DR PIR; S74712; S74712.
DR AlphaFoldDB; P72848; -.
DR SMR; P72848; -.
DR STRING; 1148.1651937; -.
DR PaxDb; P72848; -.
DR EnsemblBacteria; BAA16863; BAA16863; BAA16863.
DR KEGG; syn:sll1185; -.
DR eggNOG; COG0408; Bacteria.
DR InParanoid; P72848; -.
DR OMA; HDKGTLF; -.
DR PhylomeDB; P72848; -.
DR BRENDA; 1.3.3.3; 382.
DR UniPathway; UPA00251; UER00322.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IMP:UniProtKB.
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 Chlorophyll biosynthesis; Cytoplasm; Heme biosynthesis; Manganese;
KW Metal-binding; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..340
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT /id="PRO_0000109925"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..313
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 113
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 123
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 125..127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 187
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 296..298
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT SITE 187
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ SEQUENCE 340 AA; 38937 MW; 9156238D899587FD CRC64;
MTVSPTTQPQ TNHSLPPADA KQRVSQFMQT LQDEICQGLE ALDGKGKFQE DSWQREEGGG
GRSRVLADGD FLEQGGVNFS EVWGKSLPPS ILKQRPEAEG HEFYATGTSM VLHPKNPYIP
TVHLNYRYFE AGPVWWFGGG ADLTPYYPFA EDAAHFHHTL KNACDQTHGE FYPVFKRWCD
EYFYLKHRQE MRGIGGIFFD YQDGNAPLYR GPDPNGPAAQ YSNQLAPIEP LGWEDLFSFA
QRCGRAFLPA YSPIVEKRRN TEYGDRQRQF QLYRRGRYVE FNLVYDRGTI FGLQTNGRTE
SILMSLPPLV RWQYCYSPEA GSPEAELTEK FLVPQDWVNS
