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Database: UniProt
Entry: A0A328X0M5_9FLAO
LinkDB: A0A328X0M5_9FLAO
Original site: A0A328X0M5_9FLAO 
ID   A0A328X0M5_9FLAO        Unreviewed;       452 AA.
AC   A0A328X0M5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167};
DE            EC=1.3.98.3 {ECO:0000256|PIRNR:PIRNR000167};
GN   ORFNames=B0I10_101128 {ECO:0000313|EMBL:RAR50956.1};
OS   Flavobacterium lacus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1353778 {ECO:0000313|EMBL:RAR50956.1, ECO:0000313|Proteomes:UP000249518};
RN   [1] {ECO:0000313|EMBL:RAR50956.1, ECO:0000313|Proteomes:UP000249518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12504 {ECO:0000313|EMBL:RAR50956.1,
RC   ECO:0000313|Proteomes:UP000249518};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-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:RAR50956.1}.
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DR   EMBL; QLSV01000001; RAR50956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328X0M5; -.
DR   OrthoDB; 9808022at2; -.
DR   UniPathway; UPA00251; UER00323.
DR   Proteomes; UP000249518; 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; 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; 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|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2};
KW   Cytoplasm {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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR000167}.
FT   DOMAIN          44..279
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         53
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         59
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         63
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         65..67
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         66
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         110
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         111..112
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         143
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         170
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         182
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         207
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         241
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         328
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   452 AA;  52715 MW;  3863C9AFEA946F73 CRC64;
     MSLIQKYNVP GPRYTSYPTV PYWDEDGFSV ADWKETLKKS FLQSNTAEGI SLYIHLPFCE
     SLCTFCGCNK RITKRHDVEN PYIEAVLKEW QLYCELLPKK PIIREIHLGG GTPTFFSPEN
     LERLINGLFE NATKHPNHEF SFEGHPNNTT RTHLQKLFDL GFRRVSFGVQ DYSETVQKAI
     HRIQSFHNVA KVTFWAREIG YTSVGHDLIF GLPFQTVEDV IDTIDKTNSL QPDRLAFYSY
     AHVPWIKGNG QRGFKDDDLP KDEEKRMLYE LGKKRLSENG YHEIGMDHFA LETDSLYHSF
     QERKLHRNFM GYTSSKTQVM IGLGLSSISD SWYSFAQNVK TLEEYYVCLA ENELPVFRGH
     LLTDEDLIIR KHILNIMCQL HTSWHEYGFY FSEINQVLER LHEMEEDGLV IITNHSLTVT
     EKGKPYIRNI CMAFDLRMNR NKPETKLFSM TV
//
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