CTAA_STAHJ
ID CTAA_STAHJ Reviewed; 304 AA.
AC Q4L5C9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SH1837;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05146.1; -; Genomic_DNA.
DR RefSeq; WP_011276113.1; NC_007168.1.
DR AlphaFoldDB; Q4L5C9; -.
DR SMR; Q4L5C9; -.
DR STRING; 279808.SH1837; -.
DR EnsemblBacteria; BAE05146; BAE05146; SH1837.
DR GeneID; 58062040; -.
DR KEGG; sha:SH1837; -.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_041525_3_1_9; -.
DR OMA; YTGAYVR; -.
DR OrthoDB; 1135592at2; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000000543; 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..304
FT /note="Heme A synthase"
FT /id="PRO_0000349003"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 94..114
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 216..236
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 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT BINDING 214
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 276
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 304 AA; 34390 MW; C6C5DBF2E972BF74 CRC64;
MFNKRNLKWL SVLATIIMAF VQLGGALVTK TGSEDGCGSS WPLCHGALLP QNLPIDTIIE
LSHRAVSGLS LIVVLWLAIT AWKHIGYIRE VKPLAIISIA FLLVQALIGA AAVIWQQNSY
VLALHFGISL ISFSSVFVLM LIIFEVDKKY EADELYIRKP LRRLTWIMTG IVYLTIYTGA
LVRHAKASLA YGGWPLPFHD IIPHTEQDWV QFAHRGMAFI TFFWIMITFI HAVKNYSENR
TIRYGYTTAF ILIILQVITG ALSVMTNVNL FIALLHALFI TILFGMIAYF IMLMLRTIRS
EKIK
