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HEMN_AQUAE
ID   HEMN_AQUAE              Reviewed;         456 AA.
AC   O67886;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Oxygen-independent coproporphyrinogen III oxidase;
DE            Short=CPO;
DE            EC=1.3.98.3 {ECO:0000250|UniProtKB:P32131};
DE   AltName: Full=Coproporphyrinogen III dehydrogenase;
DE            Short=CPDH;
GN   Name=hemN; OrderedLocusNames=aq_2124;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the anaerobic
CC       oxidative decarboxylation of propionate groups of rings A and B of
CC       coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen
CC       IX. {ECO:0000250|UniProtKB:P32131}.
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:0000250|UniProtKB:P32131};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P32131};
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};
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   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07846.1; -; Genomic_DNA.
DR   PIR; B70482; B70482.
DR   RefSeq; NP_214455.1; NC_000918.1.
DR   RefSeq; WP_010881391.1; NC_000918.1.
DR   AlphaFoldDB; O67886; -.
DR   SMR; O67886; -.
DR   STRING; 224324.aq_2124; -.
DR   EnsemblBacteria; AAC07846; AAC07846; aq_2124.
DR   KEGG; aae:aq_2124; -.
DR   PATRIC; fig|224324.8.peg.1639; -.
DR   eggNOG; COG0635; Bacteria.
DR   HOGENOM; CLU_027579_3_0_0; -.
DR   InParanoid; O67886; -.
DR   OMA; HILNLMC; -.
DR   OrthoDB; 1130951at2; -.
DR   UniPathway; UPA00251; UER00323.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; ISS: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:0006779; P:porphyrin-containing compound biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; ISS: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   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..456
FT                   /note="Oxygen-independent coproporphyrinogen III oxidase"
FT                   /id="PRO_0000109938"
FT   DOMAIN          46..280
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         61
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         65
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         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         68
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         112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         113..114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         184
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         243
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         329
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
SQ   SEQUENCE   456 AA;  53785 MW;  4E494103B8EF6342 CRC64;
     MKAEFDKELI KKYDRPGPRY TSYPPATEFT EEVKEDEYVK RLIKSNERKT PLSLYFHIPF
     CEQRCLYCGC NVIISHRKGI EEPYLERVCR EMDLVSQYLD KDRKVIQLHW GGGTPNYLSP
     EQIKWFMEEI RKRFEFGDNA EISIELDPRY LTDEQIKAIK DAGFNRISLG VQDLDPKVQQ
     AVNRVQPYEL IKEKMEKLRE AGFESINLDL IYGLPYQTKE SFEKTVEKVI ELNPDRIATY
     SFAYIPQVKP HQQLLPKEAL PSAEEKLRIF EMVINKFQEA GYVYIGMDHF AKPEDELAVA
     QRKGELWRNF QGYTTKKGVE LLGFGATSIG MLYDSYFQNW KTLRDYNKTV DEGKIPVFRG
     YVLNEDDFIR REVIMDIMCN LGVEFSKIEN MFGINFREYF AKELEELKEM EEDGLIKVEE
     DRIKIMPVGR LLIRNVAMVF DAHLRRKKEL NFSRTI
 
 
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