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CTAA_BACLD
ID   CTAA_BACLD              Reviewed;         302 AA.
AC   Q65K14; Q62VG5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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};
GN   OrderedLocusNames=BLi01704, BL02999;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU23243.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU40600.1; -; Genomic_DNA.
DR   RefSeq; WP_003181473.1; NC_006322.1.
DR   AlphaFoldDB; Q65K14; -.
DR   SMR; Q65K14; -.
DR   STRING; 279010.BL02999; -.
DR   DNASU; 3030841; -.
DR   EnsemblBacteria; AAU23243; AAU23243; BL02999.
DR   GeneID; 66216282; -.
DR   KEGG; bld:BLi01704; -.
DR   KEGG; bli:BL02999; -.
DR   eggNOG; COG1612; Bacteria.
DR   HOGENOM; CLU_041525_3_1_9; -.
DR   OMA; YTGAYVR; -.
DR   OrthoDB; 1135592at2; -.
DR   BioCyc; BLIC279010:BLI_RS08435-MON; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000000606; 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..302
FT                   /note="Heme A synthase"
FT                   /id="PRO_0000348973"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        62..82
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        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        273..293
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   302 AA;  33298 MW;  279D50BACE899311 CRC64;
     MNKALKGLGI ITTIAMLFVL IGGALVTKTG SGMGCGRSWP LCNGSIFPAL TLESIIEWSH
     RFVSGTSGVL VLALAIWTWK KIGHIRETKF LAVMSVVFLI LQALLGAAAV VFGSSALIMA
     LHFGISLISF ASVLLLTLLV FEADSKQKSE SFYIGKTMQF HMIGIIIYTY VVVYTGAYVR
     HTSSSLACLD FPMCSTENGW LPGKFHEWVQ MGHRAAALLL FAWIIAAAVH AARQYKNQKR
     IYWGWMISLI LIILQAASGI AVVYSRLDLG FALAHAFFIS CLFGILCYFL LLVARYRRQV
     QK
 
 
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