CTAA_ALKHC
ID CTAA_ALKHC Reviewed; 298 AA.
AC Q9K9M8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=BH2617;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06336.1; -; Genomic_DNA.
DR PIR; A83977; A83977.
DR RefSeq; WP_010898768.1; NC_002570.2.
DR AlphaFoldDB; Q9K9M8; -.
DR SMR; Q9K9M8; -.
DR STRING; 272558.10175238; -.
DR DNASU; 892546; -.
DR EnsemblBacteria; BAB06336; BAB06336; BAB06336.
DR KEGG; bha:BH2617; -.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_041525_3_0_9; -.
DR OMA; YTGAYVR; -.
DR OrthoDB; 1135592at2; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000001258; 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..298
FT /note="Heme A synthase"
FT /id="PRO_0000348972"
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 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 118..138
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 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 245..265
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 212
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 274
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 298 AA; 32445 MW; 10D0A387A1453A7B CRC64;
MHRSLKIFGT LTSIGMVIVL MQGALVTKTE SGEGCGATWP LCFGEVIPTN PAIETIIEYS
HRIVSGLLGA MVIILAIWAW RKLSHIRETK VMAILAVLFI IFQGLLGAGA VVFGQSHAIL
ALHFGISAIS LATVVLLTTL AFEDGKPNPP ALIVKKGYKG YILAVFAYCY AVIYTGAYVK
HTQATLACGD FPLCNGQWIP MLSGPVGAHF FHRVAGTLLL ILLVVALIWT LRKYSHYRSL
VWTHILCVIL VLTQYATGIS IVLTGNELFV AMMHALIVSI LFTTLCYIVM ILSRNKAV
