HEM6_SOYBN
ID HEM6_SOYBN Reviewed; 385 AA.
AC P35055;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase, chloroplastic;
DE Short=Coprogen oxidase;
DE Short=Coproporphyrinogenase;
DE EC=1.3.3.3;
DE Flags: Precursor;
GN Name=CPX;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Evans; TISSUE=Root nodule;
RX PubMed=8219054; DOI=10.1007/bf00021417;
RA Madsen O., Sandal L., Sandal N.N., Marcker K.A.;
RT "A soybean coproporphyrinogen oxidase gene is highly expressed in root
RT nodules.";
RL Plant Mol. Biol. 23:35-43(1993).
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 (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Probably regulated by oxygen tension.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in nodules and to a lesser extent
CC in leaves. Not detected in roots.
CC -!- DEVELOPMENTAL STAGE: Expression starts 10-12 days after infection and
CC continues during the lifetime of the nodule.
CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
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DR EMBL; X71083; CAA50401.1; -; Genomic_DNA.
DR EMBL; X71083; CAA50400.1; -; Genomic_DNA.
DR PIR; S39523; S39523.
DR AlphaFoldDB; P35055; -.
DR SMR; P35055; -.
DR STRING; 3847.GLYMA14G00620.2; -.
DR PRIDE; P35055; -.
DR ProMEX; P35055; -.
DR eggNOG; KOG1518; Eukaryota.
DR InParanoid; P35055; -.
DR BioCyc; MetaCyc:MON-11768; -.
DR UniPathway; UPA00251; UER00322.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.1500.10; -; 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 2: Evidence at transcript level;
KW Chlorophyll biosynthesis; Chloroplast; Heme biosynthesis; Oxidoreductase;
KW Plastid; Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..385
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase,
FT chloroplastic"
FT /id="PRO_0000006033"
FT REGION 124..133
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT REGION 325..360
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343..348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 260
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 385 AA; 43265 MW; C3FE1163CF80A09B CRC64;
MMHCASIVSA PSYAFPFRSG SASTTPTAIS LTKRSWKPPP SMAKGPVRAT VSIEKETPEA
NRPETFLRGV DEAQSSTSVR ARFEKMIREA QDTVCSALEA ADGGAQFKED VWSRPGGGGG
ISRVLQDGAV WEKAGVNVSV VYGVMPPDAY RAAKGVPTDQ KPGPVPFFAA GISSVLHPKN
PFAPTLHFNY RYFETDAPKD APGAPRQWWF GGGTDLTPAY IFEEDVKHFH SIQKQACDKF
EPTFYPRFKK WCDDYFYIKH RGERRGLGGI FFDDLNDYDQ EMLLSFATEC ANSVIPAYLP
IIEKRKDLPF NDHQKAWQQL RRGRYVEFNL VYDRGTTFGL KTGGRIESIL VSLPLTARWE
YDHKPEEGSE EWKLLDACIN PKEWI