CTAA_MARMM
ID CTAA_MARMM Reviewed; 341 AA.
AC Q0APH6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Heme A synthase {ECO:0000255|HAMAP-Rule:MF_01665};
DE Short=HAS {ECO:0000255|HAMAP-Rule:MF_01665};
DE EC=1.17.99.9 {ECO:0000255|HAMAP-Rule:MF_01665};
DE AltName: Full=Cytochrome aa3-controlling protein {ECO:0000255|HAMAP-Rule:MF_01665};
GN Name=ctaA {ECO:0000255|HAMAP-Rule:MF_01665}; OrderedLocusNames=Mmar10_1519;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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_01665}.
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_01665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63389;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01665};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01665};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis;
CC heme A from heme O: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01665}.
CC -!- SUBUNIT: Interacts with CtaB. {ECO:0000255|HAMAP-Rule:MF_01665}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01665};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01665}.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01665}.
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DR EMBL; CP000449; ABI65811.1; -; Genomic_DNA.
DR RefSeq; WP_011643458.1; NC_008347.1.
DR AlphaFoldDB; Q0APH6; -.
DR SMR; Q0APH6; -.
DR STRING; 394221.Mmar10_1519; -.
DR EnsemblBacteria; ABI65811; ABI65811; Mmar10_1519.
DR KEGG; mmr:Mmar10_1519; -.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_017627_0_0_5; -.
DR OMA; YWWEWGH; -.
DR OrthoDB; 1135592at2; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000001964; 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_01665; HemeA_synth_type2; 1.
DR InterPro; IPR003780; COX15/CtaA_fam.
DR InterPro; IPR023754; HemeA_Synthase_type2.
DR PANTHER; PTHR23289; PTHR23289; 1.
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..341
FT /note="Heme A synthase"
FT /id="PRO_0000349042"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 261..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT BINDING 259
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_01665"
FT BINDING 319
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_01665"
SQ SEQUENCE 341 AA; 37712 MW; E4D1D70EFA14C160 CRC64;
MPYHSSTKSR AVSTWLLVVA ALVCAMIIIG GTTRLTDSGL SITEWKPISG AIPPLSQQDW
QDEFALYQQT TEFQVQNSAM TLDEFEFIFW WEWGHRQLGR LIGLVYFVPF VFFWMRGHLS
ARLKSRLFGL FLLGGAQGAI GWWMVASGLS DRLDVSQYRL ATHLGMAFVI LGLSIWFSLE
ARHGPPPLRR GRLAGVTAGL LGLVFVQIIL GAFVAGLDAG RIYNTWPLMN GDLIPEGYLG
GMNFFPAIFE SHAAVQMHHR WTGYLVALGV FAYAWQVWRE PRVSLKPFMV ILPALVIGQI
ALGIAALLAV VPLSLSLAHQ AGAILLFIAM VAAAWTARRA V
