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CTAA_MACCJ
ID   CTAA_MACCJ              Reviewed;         300 AA.
AC   B9EB26;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=MCCL_0730;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(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}.
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DR   EMBL; AP009484; BAH17437.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9EB26; -.
DR   SMR; B9EB26; -.
DR   STRING; 458233.MCCL_0730; -.
DR   EnsemblBacteria; BAH17437; BAH17437; MCCL_0730.
DR   KEGG; mcl:MCCL_0730; -.
DR   eggNOG; COG1612; Bacteria.
DR   HOGENOM; CLU_041525_3_1_9; -.
DR   OMA; YTGAYVR; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000001383; 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; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..300
FT                   /note="Heme A synthase"
FT                   /id="PRO_1000187243"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   BINDING         216
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         278
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   300 AA;  33897 MW;  3FA414F85B19CB3B CRC64;
     MLKEKNLKWL SLFTTVLMLF VQIGGALVTK TGSADGCGSS WPLCHGKFVP THIPKETLIE
     LAHRGVSGLA LLSVTWLVIL SIKYIGHKKE TKFLCYMSIG FIFAQALIGA AAVMWQQNGF
     VLALHFGISL ISFSAVFLLT LLIFEVDQKF DATKLILQPK LRRHTIGLTS FIYFVIYSGA
     LVRHEKASLA CSSWPLCRKG AFILPQNFYE WVQMSHRTLA FILFIWLTYV AFHAMRNYAQ
     YRVIKYGYMI AFILICLQVT TGALTIFTAV NLYIALLHAL FITLLFGLLC YFILLISRAK
 
 
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