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CTAA_LISMH
ID   CTAA_LISMH              Reviewed;         305 AA.
AC   B8DH71;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=LMHCC_0502;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK38859.1; -; Genomic_DNA.
DR   RefSeq; WP_003723941.1; NC_011660.1.
DR   AlphaFoldDB; B8DH71; -.
DR   SMR; B8DH71; -.
DR   GeneID; 61171350; -.
DR   KEGG; lmh:LMHCC_0502; -.
DR   HOGENOM; CLU_041525_3_1_9; -.
DR   OMA; YTGAYVR; -.
DR   UniPathway; UPA00269; UER00713.
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..305
FT                   /note="Heme A synthase"
FT                   /id="PRO_1000187242"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        64..84
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        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT   TRANSMEM        241..261
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         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   305 AA;  34567 MW;  30DFA21331BC1ED1 CRC64;
     MKKFLKVWSV LTIICMTVVV FGGALVTKTG SADGCGNSWP LCNGQLVRLT DVTPEKLIEF
     MHRMTTGISS IFVIVLAICA WIYMKNRRET KPLAIIAVLF LIIQALMGMA AVVWGQNPYI
     MALHFGISII CYASIVLLAL MIFEVDRKFD ARNLVMGTKL RINIYALTIY TYLAVYTGAL
     VRHEKASMAV PVWPFENGHF IMPTSVQDYV QYFHRLAAFI LIVWLLYVTW LVFRDYRRYR
     VLTFSMVLSL VFIALQAVTG ALSVYTGVNL YIALAHSLII TMLFALLCYL CLLASRSKSN
     RLRIK
 
 
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