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CTAA_BACCR
ID   CTAA_BACCR              Reviewed;         311 AA.
AC   Q819N0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=BC_3946;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP10866.1; -; Genomic_DNA.
DR   RefSeq; NP_833665.1; NC_004722.1.
DR   RefSeq; WP_001188743.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q819N0; -.
DR   SMR; Q819N0; -.
DR   STRING; 226900.BC_3946; -.
DR   EnsemblBacteria; AAP10866; AAP10866; BC_3946.
DR   GeneID; 67508580; -.
DR   KEGG; bce:BC3946; -.
DR   PATRIC; fig|226900.8.peg.4070; -.
DR   HOGENOM; CLU_041525_3_1_9; -.
DR   OMA; YTGAYVR; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000001417; 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..311
FT                   /note="Heme A synthase"
FT                   /id="PRO_0000348968"
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;  34623 MW;  BFCBC307152DDDB2 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 LVTLQAVVGV LVVFTNASLA MALLHSLFIS CLFAVLCYLV MLGTRSKVNA
     KEAELTSKQT K
 
 
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