位置:首页 > 蛋白库 > CTAA_BACCQ
CTAA_BACCQ
ID   CTAA_BACCQ              Reviewed;         311 AA.
AC   B9IW25;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Heme A synthase {ECO:0000255|HAMAP-Rule:MF_01664};
DE            Short=HAS {ECO:0000255|HAMAP-Rule:MF_01664};
DE            EC=1.17.99.9 {ECO:0000255|HAMAP-Rule:MF_01664};
DE   AltName: Full=Cytochrome aa3-controlling protein {ECO:0000255|HAMAP-Rule:MF_01664};
GN   Name=ctaA {ECO:0000255|HAMAP-Rule:MF_01664}; OrderedLocusNames=BCQ_3734;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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_01664}.
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_01664};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63389;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01664};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01664};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis;
CC       heme A from heme O: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01664}.
CC   -!- SUBUNIT: Interacts with CtaB. {ECO:0000255|HAMAP-Rule:MF_01664}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01664};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01664}.
CC   -!- SIMILARITY: Belongs to the COX15/CtaA family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01664}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000227; ACM14162.1; -; Genomic_DNA.
DR   RefSeq; WP_001188736.1; NC_011969.1.
DR   AlphaFoldDB; B9IW25; -.
DR   SMR; B9IW25; -.
DR   EnsemblBacteria; ACM14162; ACM14162; BCQ_3734.
DR   GeneID; 64199287; -.
DR   KEGG; bcq:BCQ_3734; -.
DR   HOGENOM; CLU_041525_3_1_9; -.
DR   OMA; YTGAYVR; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000000441; 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_01664; HemeA_synth_type1; 1.
DR   InterPro; IPR003780; COX15/CtaA_fam.
DR   InterPro; IPR023755; HemeA_Synthase_type1.
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..311
FT                   /note="Heme A synthase"
FT                   /id="PRO_1000187241"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   BINDING         213
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_01664"
FT   BINDING         275
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_01664"
SQ   SEQUENCE   311 AA;  34595 MW;  5BC36ACB645189FF CRC64;
     MQRFIKWLAV ITSLDLLIVL LGGALVTKTG SGQGCGKSWP LCNGEFVPSN LSMETIIELS
     HRLTSGSAGI LVTLLCILSW KYYKHVRETK TLAILSFVFL VAQALMGAAA VVWGQMPAVL
     AIHFGISLIS FASVILLTCL IFEIDQKFDA RSLIMDKKMK FHIYGVTIYS YIVVYTGALV
     RHERASLACP DFPLCSKNRP MPTQLHEWVQ MGHRVAAMLI FAWILYAMIL AIRHYKQQPV
     VYWGWIISFI LVTLQAIVGI LVVFTNASLS MALLHSLFIS CLFAVLCYLV MLGTRSKVNA
     KEAASISKQT K
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024