HEMN_SYNY3
ID HEMN_SYNY3 Reviewed; 466 AA.
AC P74132;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Oxygen-independent coproporphyrinogen III oxidase;
DE Short=CPO;
DE EC=1.3.98.3 {ECO:0000269|PubMed:20194361};
DE AltName: Full=Coproporphyrinogen III dehydrogenase;
DE Short=CPDH;
GN Name=hemN; OrderedLocusNames=sll1876;
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, INDUCTION, AND
RP COFACTOR.
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 anaerobic oxidative decarboxylation of propionate groups of rings A
CC and B of coproporphyrinogen III to yield the vinyl groups in
CC protoporphyrinogen IX. {ECO:0000269|PubMed:20194361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-
CC deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX;
CC Xref=Rhea:RHEA:15425, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:57307, ChEBI:CHEBI:57309, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789; EC=1.3.98.3;
CC Evidence={ECO:0000269|PubMed:20194361};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P32131, ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:P32131, ECO:0000305};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet
CC route): step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P32131}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32131}.
CC -!- INDUCTION: Induced under microoxic conditions.
CC {ECO:0000269|PubMed:20194361}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow significantly slower
CC than that of the wild-type under microoxic conditions, while they grow
CC normally under aerobic conditions. Coproporphyrin-III is accumulated at
CC a low but significant level in the mutant growing under microoxic
CC conditions. {ECO:0000269|PubMed:20194361}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18218.1; -; Genomic_DNA.
DR PIR; S75657; S75657.
DR AlphaFoldDB; P74132; -.
DR SMR; P74132; -.
DR STRING; 1148.1653303; -.
DR PaxDb; P74132; -.
DR EnsemblBacteria; BAA18218; BAA18218; BAA18218.
DR KEGG; syn:sll1876; -.
DR eggNOG; COG0635; Bacteria.
DR InParanoid; P74132; -.
DR OMA; HILNLMC; -.
DR PhylomeDB; P74132; -.
DR UniPathway; UPA00251; UER00323.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR004558; Coprogen_oxidase_HemN.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000167; HemN; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00538; hemN; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Chlorophyll biosynthesis; Cytoplasm; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Porphyrin biosynthesis; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..466
FT /note="Oxygen-independent coproporphyrinogen III oxidase"
FT /id="PRO_0000109954"
FT DOMAIN 51..285
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 118..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 214
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 334
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 466 AA; 53161 MW; D49735A905A5C572 CRC64;
MTTTFPTVEF SAELLNKYNQ GIPRYTSYPP ATELNKEFDP SDFQTAINLG NYKKTPLSLY
CHIPFCAKAC YFCGCNTIIT QHKPAVDPYL KAVAKQIALV APLVDQQRPV QQLHWGGGTP
NYLTLEQAEF LFNTITDAFP LAENAEISIE INPCYVDKDY IFALRQLGFN RISFGIQDFN
SQVQQAVNRI QPEAMLFQVM DWIRQANFDS VNVDLIYGLP HQNLATFRET LRKTAQLNPD
RIAVFNFAYV PWLKPVQKKM PESALPPAEE KLKIMQATIA DLTEQGYVFI GMDHFAKPDD
ELAIAQRRGE LHRNFQGYTT QPESDLLGFG ITSISMLQDV YAQNHKTLKA FYNALDREVM
PIEKGFKLSQ DDLIRRTVIK ELMCQFKLSA QELESKYNLG FDCDFNDYFA KELSALDVLE
ADGLLRRLGD GLEVTPRGRI LIRNIAAVFD TYLQNKSKQQ MFSRAI
