CTAA_BACC1
ID CTAA_BACC1 Reviewed; 311 AA.
AC Q732C1; Q9XBJ0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=BCE_3993;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10217496; DOI=10.1099/13500872-145-3-621;
RA Oekstad O.A., Hegna I.K., Lindbaeck T., Rishovd A.-L., Kolstoe A.-B.;
RT "Genome organization is not conserved between Bacillus cereus and Bacillus
RT subtilis.";
RL Microbiology 145:621-631(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(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; AJ010111; CAB40605.1; -; Genomic_DNA.
DR EMBL; AE017194; AAS42896.1; -; Genomic_DNA.
DR PIR; T44610; T44610.
DR RefSeq; WP_001188737.1; NC_003909.8.
DR AlphaFoldDB; Q732C1; -.
DR SMR; Q732C1; -.
DR EnsemblBacteria; AAS42896; AAS42896; BCE_3993.
DR GeneID; 59155492; -.
DR KEGG; bca:BCE_3993; -.
DR HOGENOM; CLU_041525_3_1_9; -.
DR OMA; YTGAYVR; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000002527; 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_0000348967"
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"
FT CONFLICT 252
FT /note="V -> D (in Ref. 1; CAB40605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34583 MW; 5BC36ACB644079FF 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
KEAASTSKQT K
