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NIRDL_PARPN
ID   NIRDL_PARPN             Reviewed;         326 AA.
AC   I6UH61;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Siroheme decarboxylase NirDL subunit {ECO:0000305};
DE            EC=4.1.1.111 {ECO:0000269|PubMed:21969545};
GN   Name=nirDL {ECO:0000303|PubMed:21969545};
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=82367;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC   82005 / GB17;
RX   PubMed=21969545; DOI=10.1073/pnas.1108228108;
RA   Bali S., Lawrence A.D., Lobo S.A., Saraiva L.M., Golding B.T., Palmer D.J.,
RA   Howard M.J., Ferguson S.J., Warren M.J.;
RT   "Molecular hijacking of siroheme for the synthesis of heme and d1 heme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:18260-18265(2011).
CC   -!- FUNCTION: Involved in heme d1 biosynthesis. Catalyzes the
CC       decarboxylation of siroheme into didecarboxysiroheme (PubMed:21969545).
CC       Siroheme is probably decarboxylated to monodecarboxysiroheme, which is
CC       in turn decarboxylated to didecarboxysiroheme (PubMed:21969545).
CC       {ECO:0000269|PubMed:21969545}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2;
CC         Xref=Rhea:RHEA:19093, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:60052, ChEBI:CHEBI:140497; EC=4.1.1.111;
CC         Evidence={ECO:0000269|PubMed:21969545};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism.
CC       {ECO:0000269|PubMed:21969545}.
CC   -!- SUBUNIT: Forms a complex composed of NirDL, NirG and NirH. All proteins
CC       are required for the total conversion of siroheme to
CC       didecarboxysiroheme. {ECO:0000269|PubMed:21969545}.
CC   -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR   EMBL; JQ922108; AFM94357.1; -; Genomic_DNA.
DR   AlphaFoldDB; I6UH61; -.
DR   SMR; I6UH61; -.
DR   BioCyc; MetaCyc:MON-18861; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000485; AsnC-type_HTH_dom.
DR   InterPro; IPR040523; AsnC_trans_reg2.
DR   InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR   InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF17805; AsnC_trans_reg2; 2.
DR   Pfam; PF13404; HTH_AsnC-type; 1.
DR   SMART; SM00344; HTH_ASNC; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   Lyase.
FT   CHAIN           1..326
FT                   /note="Siroheme decarboxylase NirDL subunit"
FT                   /id="PRO_0000450515"
SQ   SEQUENCE   326 AA;  35611 MW;  C8FF08C0DB94A70C CRC64;
     MTMDDLDLRL LDGFQRDLPL ETRPFAAIAN RLNTSEAEVI ARLARLRDEG LIARIGATCR
     PNTAGASTLA ALRVPVRRID KVAALVGAEP GVNHSYLREG SDWNLWFVAT APDAEALEES
     LVRIETATGL VPLSLPLVRA FNIDLGFPLI GPRRAMALDR PTDLDVLRPR DKALMQALTT
     GLALVPRPFV ALGQALGRSE AEVISRIRAL AAARILTRVG VIVRHRALGW CENAMVVWRL
     PEPAVEAAGT ALAAVPGVTL CYQRRTVPGL WNWPLFCMIH ARSRAEAMEV LVQARALPEL
     QGVPHRILFS TRCFRQRGAV IAEVAA
 
 
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