ID A0A433SBS6_9BURK Unreviewed; 461 AA.
AC A0A433SBS6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167};
DE EC=1.3.98.3 {ECO:0000256|PIRNR:PIRNR000167};
GN Name=hemN_3 {ECO:0000313|EMBL:RUS66208.1};
GN ORFNames=CUZ56_02287 {ECO:0000313|EMBL:RUS66208.1};
OS Saezia sanguinis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Saezia.
OX NCBI_TaxID=1965230 {ECO:0000313|EMBL:RUS66208.1, ECO:0000313|Proteomes:UP000286947};
RN [1] {ECO:0000313|EMBL:RUS66208.1, ECO:0000313|Proteomes:UP000286947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNM695-12 {ECO:0000313|EMBL:RUS66208.1,
RC ECO:0000313|Proteomes:UP000286947};
RA Medina-Pascual M.J., Valdezate S., Monzon S., Cuesta I., Carrasco G.,
RA Villalon P., Saez-Nieto J.A.;
RT "Saezia sanguinis gen. nov., sp. nov., in the order Burkholderiales
RT isolated from human blood.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001496,
CC ECO:0000256|PIRNR:PIRNR000167};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR000167,
CC ECO:0000256|PIRSR:PIRSR000167-2};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004785,
CC ECO:0000256|PIRNR:PIRNR000167}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR000167}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000256|ARBA:ARBA00005493, ECO:0000256|PIRNR:PIRNR000167}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUS66208.1}.
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DR EMBL; PQSP01000006; RUS66208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433SBS6; -.
DR OrthoDB; 9808022at2; -.
DR UniPathway; UPA00251; UER00323.
DR Proteomes; UP000286947; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 1.10.10.920; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004558; Coprogen_oxidase_HemN.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00538; hemN; 1.
DR PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR PANTHER; PTHR13932:SF6; OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000167; HemN; 1.
DR SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR000167};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000167};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000167};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR000167};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000167};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000167};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|PIRNR:PIRNR000167};
KW Reference proteome {ECO:0000313|Proteomes:UP000286947};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR000167}.
FT DOMAIN 50..284
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-2"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-2"
FT BINDING 71..73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-2"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
SQ SEQUENCE 461 AA; 52739 MW; 4D2985CE769B2496 CRC64;
MQQLVITPEL LRRYDVSGPR YTSYPTADRF VEAFDEADYL QALTQRTVGA IAANPLSIYV
HIPFCESLCY YCGCNKIVTK HHERALPYLE GLLKEMALVA KQLDSRQRVS QIHFGGGSPT
FLSDEELSQV MSKLREHFEF MDSLECTIEV DPRTVSRERL QNLWDMGFNR LSLGIQDFDH
QVQQAIHRVQ STESVFALMQ AARDIGFTSI SVDLIYGLPK QTQASFNETL DQIAVLRPDR
IAVYGYAHLP SRFKPQRRIH NEDLPDGATR LNLMSESISR LQKAGYEYIG MDHFALPEDS
LSVAKRHGRM HRNFQGYSTH ADCDLIGLGI SAISKVGAVY SQNAKELEDY MDQVEQGHLP
VMRGYALDRD DLVRRAVISA IMCQGVIIYE SIELAYLVDF KSYFAKELAQ LQPFVEQGLM
EFDENGFRVK SLGWYFVRAL AMTFDKYLQA DLTRERFSRI I
//
