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CTAA_METS4
ID   CTAA_METS4              Reviewed;         360 AA.
AC   B0UR12;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Heme A synthase {ECO:0000255|HAMAP-Rule:MF_01665};
DE            Short=HAS {ECO:0000255|HAMAP-Rule:MF_01665};
DE            EC=1.17.99.9 {ECO:0000255|HAMAP-Rule:MF_01665};
DE   AltName: Full=Cytochrome aa3-controlling protein {ECO:0000255|HAMAP-Rule:MF_01665};
GN   Name=ctaA {ECO:0000255|HAMAP-Rule:MF_01665}; OrderedLocusNames=M446_5367;
OS   Methylobacterium sp. (strain 4-46).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4-46;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of heme O to heme A by two
CC       successive hydroxylations of the methyl group at C8. The first
CC       hydroxylation forms heme I, the second hydroxylation results in an
CC       unstable dihydroxymethyl group, which spontaneously dehydrates,
CC       resulting in the formyl group of heme A. {ECO:0000255|HAMAP-
CC       Rule:MF_01665}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a;
CC         Xref=Rhea:RHEA:63388, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:60530, ChEBI:CHEBI:61715;
CC         EC=1.17.99.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01665};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63389;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01665};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01665};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis;
CC       heme A from heme O: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01665}.
CC   -!- SUBUNIT: Interacts with CtaB. {ECO:0000255|HAMAP-Rule:MF_01665}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01665};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01665}.
CC   -!- SIMILARITY: Belongs to the COX15/CtaA family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01665}.
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DR   EMBL; CP000943; ACA19685.1; -; Genomic_DNA.
DR   RefSeq; WP_012335070.1; NC_010511.1.
DR   AlphaFoldDB; B0UR12; -.
DR   SMR; B0UR12; -.
DR   STRING; 426117.M446_5367; -.
DR   EnsemblBacteria; ACA19685; ACA19685; M446_5367.
DR   KEGG; met:M446_5367; -.
DR   eggNOG; COG1612; Bacteria.
DR   HOGENOM; CLU_017627_0_0_5; -.
DR   OMA; YWWEWGH; -.
DR   OrthoDB; 1135592at2; -.
DR   UniPathway; UPA00269; UER00713.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IEA:InterPro.
DR   GO; GO:0006784; P:heme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01665; HemeA_synth_type2; 1.
DR   InterPro; IPR003780; COX15/CtaA_fam.
DR   InterPro; IPR023754; HemeA_Synthase_type2.
DR   PANTHER; PTHR23289; PTHR23289; 1.
DR   Pfam; PF02628; COX15-CtaA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme biosynthesis; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..360
FT                   /note="Heme A synthase"
FT                   /id="PRO_0000349047"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   BINDING         276
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   BINDING         337
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
SQ   SEQUENCE   360 AA;  37950 MW;  20E1AF3DF06579C3 CRC64;
     MTSAALKPLS VAPARDRAAS RPRIAVRRWL FLMAALVVAM VAVGGATRLT GSGLSITEWK
     PVTGAVPPLS AEAWAEEFAK YRATPQYDIL NRGMSLAEFQ VIYAWEWGHR FLGRLIGLCF
     FLPLGWFWWT GRLDRRLGLG LVGLGVLGGL QGAVGWIMVA SGLQPGMVAV APIKLAAHLT
     LASAIFAGLV WLAAGLDRPA EAAAPRRLRL TALLLPVATL LQIALGGLVA GSKAGLTYNT
     WPLMDGAFIP PVSGLFAATP WIENFVDNVA LVQLNHRLVA YALLALALLH ALDARRARPG
     SGAARRAAAL AGLVAAQAML GITTLLLAVP LWAGLAHQVT AMLVLGMAVA HARIGTLARG
 
 
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