HEM6_LEIMA
ID HEM6_LEIMA Reviewed; 301 AA.
AC P84155;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase;
DE Short=Coprogen oxidase;
DE Short=Coproporphyrinogenase;
DE EC=1.3.3.3;
GN ORFNames=LMAJ006828, LmjF06.1270, LmjF_06_1270;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000312|EMBL:CAJ02175.1, ECO:0000312|PDB:1VJU}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-301, AND SUBUNIT.
RG Structural genomics of pathogenic protozoa consortium (SGPP);
RT "Coproporphyrinogen III oxidase from Leishmania major.";
RL Submitted (MAR-2004) to the PDB data bank.
RN [3] {ECO:0000312|EMBL:CAJ02175.1, ECO:0000312|PDB:1VJU}
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 1-301 IN COMPLEX WITH SUBSTRATE
RP ANALOG, AND SUBUNIT.
RA Merritt E.A., Le Trong I., Larson E.T., Shibata S., Zhang Z., Anderson L.,
RA Ross J., Verlinde C.L.M.J., Buckner F.S., Van Voorhis W.C., Hol G.J.W.,
RA Fan E.;
RT "Leishmania major coproporphyrinogen III oxidase with bound ligand.";
RL Submitted (JUL-2008) to the PDB data bank.
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 (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 Evidence={ECO:0000305};
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:0000269|Ref.2, ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
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DR EMBL; FR796402; CAJ02175.1; -; Genomic_DNA.
DR RefSeq; XP_001680900.1; XM_001680848.1.
DR PDB; 1VJU; X-ray; 1.40 A; A/B=1-301.
DR PDB; 2QT8; X-ray; 1.75 A; A/B=1-301.
DR PDB; 3DWR; X-ray; 1.66 A; A/B=1-301.
DR PDB; 3DWS; X-ray; 2.50 A; A/B=1-301.
DR PDBsum; 1VJU; -.
DR PDBsum; 2QT8; -.
DR PDBsum; 3DWR; -.
DR PDBsum; 3DWS; -.
DR AlphaFoldDB; P84155; -.
DR SMR; P84155; -.
DR STRING; 5664.LmjF.06.1270; -.
DR EnsemblProtists; CAJ02175; CAJ02175; LMJF_06_1270.
DR GeneID; 5649152; -.
DR KEGG; lma:LMJF_06_1270; -.
DR VEuPathDB; TriTrypDB:LmjF.06.1270; -.
DR VEuPathDB; TriTrypDB:LMJLV39_060019600; -.
DR VEuPathDB; TriTrypDB:LMJSD75_060019700; -.
DR eggNOG; KOG1518; Eukaryota.
DR InParanoid; P84155; -.
DR OMA; WFGGITD; -.
DR UniPathway; UPA00251; UER00322.
DR EvolutionaryTrace; P84155; -.
DR Proteomes; UP000000542; Chromosome 6.
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:0006782; P:protoporphyrinogen IX biosynthetic process; IBA:GO_Central.
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 3D-structure; Cytoplasm; Heme biosynthesis; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..301
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT /id="PRO_0000109876"
FT REGION 49..58
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT REGION 241..276
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT BINDING 109..111
FT /ligand="substrate"
FT BINDING 259..261
FT /ligand="substrate"
FT HELIX 2..27
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1VJU"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 54..69
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2QT8"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:2QT8"
FT STRAND 86..100
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 105..117
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 120..133
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 179..191
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 196..221
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 228..247
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1VJU"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3DWR"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:1VJU"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:1VJU"
SQ SEQUENCE 301 AA; 34370 MW; A5D8CFE90BA90435 CRC64;
MSLAVEAVKD FLLKLQDDIC EALEAEDGQA TFVEDKWTRE GGGGGRTRVM VDGAVIEKGG
VNFSHVYGKG LPMSSTERHP DIAGCNFEAM GVSLVIHPKN PHVPTSHANV RLFVAEREGK
EPVWWFGGGF DLTPYYAVEE DCRDFHQVAQ DLCKPFGADV YARFKGWCDE YFFIPYRNEA
RGIGGLFFDD LNEWPFEKCF EFVQAVGKGY MDAYIPIVNR RKNTPYTEQQ VEFQEFRRGR
YAEFNLVIDR GTKFGLQSGG RTESILISLP PRARWGYNWQ PEPGTPEARL TEYFLTKRQW
V
