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CTAA_RHIEC
ID   CTAA_RHIEC              Reviewed;         367 AA.
AC   Q2K9W9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=RHE_CH01565;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC90367.1; -; Genomic_DNA.
DR   RefSeq; WP_011424892.1; NC_007761.1.
DR   AlphaFoldDB; Q2K9W9; -.
DR   SMR; Q2K9W9; -.
DR   STRING; 347834.RHE_CH01565; -.
DR   PRIDE; Q2K9W9; -.
DR   EnsemblBacteria; ABC90367; ABC90367; RHE_CH01565.
DR   KEGG; ret:RHE_CH01565; -.
DR   eggNOG; COG1612; Bacteria.
DR   HOGENOM; CLU_017627_0_0_5; -.
DR   OMA; YWWEWGH; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000001936; Chromosome.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Heme A synthase"
FT                   /id="PRO_0000349060"
FT   TRANSMEM        25..45
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        174..194
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        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   BINDING         274
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         335
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   367 AA;  41124 MW;  D00DD3F9F1152B1E CRC64;
     MAVANLTTEQ AILSEVHKQN RNRRALRLWL GFVLLALFCL VLVGGATRLT NSGLSITEWK
     PIHGVIPPLS AAEWDEEFRL YQRIPEFQQL NSSMTVDEFK SIFWWEWAHR LIARGIGVIF
     ALPLLYFWLT GRIEKRLRWP LVGILALGAL QGFIGWWMVS SGLSVRTDVS QYRLATHLVM
     ACLIFAGCMW IMRGLSPHSN DPAPARSSRG LAAAIAVFAL FQIYLGALVA GLDAGFSYNT
     WPLMDGAVIP SDLLIQQPFW INAFENPKTV QFIHRIGAYT LFALVLINMV IALRTAPWTT
     HARRAVLLFA LVTVQAAIGV ATLLMQVPLH WGLLHQAGAL VVFGFAVANW RGFYGEYPHE
     TMIAERD
 
 
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